INSOLUBLE COMPOSITIONS FOR CONTROLLING BLOOD GLUCOSE Background of the Invention 1. Field of the Invention. This invention is in the field of human medicine. More particularly, this invention is in the field of pharmaceutical treatment of the diseases of diabetes and hyperglycemia. 2. Description of Related Art. It has long been a goal of insulin therapy to mimic the pattern of endogenous insulin secretion in normal individuals. The daily physiological demand for insulin fluctuates and can be separated into two phases: (a) the absorptive phase requiring a pulse of insulin to dispose of the meal-related blood glucose surge, and (b) the post-absorptive phase requiring a sustained delivery of insulin to regulate hepatic glucose output for maintaining optimal fasting blood glucose. Accordingly, effective therapy for people with diabetes generally involves the combined use of two types of exogenous insulin formulations: a rapid acting meal time insulin provided by bolus injections and a long-acting, so- called, basal insulin, administered by injection once or twice daily to control blood glucose levels between meals. An ideal basal insulin will provide an extended and "flat" time action - that is, it will control blood glucose levels for at least 12 hours, and preferably for 24 hours or more, without significant risk of laypoglycemia. Furthermore, an ideal basal insulin should be mixable with a soluble meal- time insulin, and should not cause irritation or reaction at the site of administration. Finally, basal insulin to be readily, and uniformly resuspended by the patient prior to administration. As is well understood by those skilled in this art, long-acting insulin formulations have been obtained by formulating normal insulin as microcrystalline suspensions for subcutaneous injection. Examples of commercial basal insulin preparations include NPH (Neutral Protamine Hagedorn) insulin, protamine zinc insulin (PZI), and ultralente »iimafcw in/nil•"" analog. B28-Ne-Pentanoyl-LysB28,ProB29-human imar!in analog. Bl-Na-Pentanoyl-LysB28,ProB29-human insulin analog. Al-Na-Pentanoyl-LysB28,ProB29-human insulin analog. B2 8 -Ne-Pentanoyl -, Bl -Na-pentanoyl - LysB28,ProB2 9-human insulin analog. B28-Ne-Pentanoyl-, Al-Na-pentanoyl-LysB28, ProB29-human insulin analog. Al-Na-Pentanoyl-, Bl-Na-pentanoyl-LysB2 8, ProB29-human insulin analog. B2 8 -Ne-Pentanoyl -, Al -Na-pentanoyl -, Bl -Na-pentanoyl- LysB28,ProB29-human insulin analog. B2 8 -Ne-Hexanoyl -LysB2 8, ProB2 9-human insulin analog. Bl-Na-Hexanoyl-LysB28,ProB29-human insulin analog. Al-Na-Hexanoyl-LysB28,ProB29-huraan insulin analog. B28-Ne-Hexanoyl-,Bl-Na-hexanoyl-LysB28, ProB29-human insulin analog. B28-Ne-Hexanoyl-,Al-Na-hexanoyl-LysB28, ProB29-human insulin analog. Al-Na-Hexanoyl-, Bl-Na-hexanoyl-LysB28, ProB29-human insulin analog. B28-Ne-Hexanoyl-, Al-Na-hexanoyl-, Bl-Na-hexanoyl- LysB28,ProB29-human insulin analog. B28-Ne-Heptanoyl-LysB28,ProB29-human insulin analog. Bl-Na-Heptanoyl-LysB28,ProB29-human insulin analog. Al-Na-Heptanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Heptanoyl-, Bl-Na-heptanoyl-LysB28, ProB29-huraan insulin analog. B28-Ne-Heptanoyl-, Al-Na-heptanoyl-LysB28, ProB29-lminan insulin analog. Al-Na-Heptanoyl-,Bl-Na-heptanoyl-LysB28, ProB29-human insulin analog. B28-Ne-Heptanoyl-, Al-Na-faeptanoyl-, Bl-Na-heptanoyl- LysB28,ProB29-human insulin analog. B28-Nc-Octanoyl-Ly8B28,ProB29-human insulin analog. Bl-Ha-Octanoyl-LysB28,ProB29-human insulin analog. Al-Na-Octanoyl-LysB28,ProB29-human insulin analog - B28-Ne-Octanoyl-,Bl-Na-octanoyl-LysB28, ProB29-taawn insulin analog. B28-Ne-Octanoyl-, Al-Na-octanoyl-I.ysB28, ProB29~hHBnan insulin analog. Al-Na-Octanoyl-,Bl-Na-octanoyl-LysB2a, ProB29-huwan insulin analog. B28-Ne-Octanoyl-, Al-Na-octanoyl-,Bl-Na-octanoyl- LysB28,ProB29-human insulin analog. B28-Ne-Nonanoyl-LysB28,ProB29-human insulin analog. Bl-Na-Nonanoyl-LysB28,ProB29-human insulin analog. Al-Na-Nonanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Nonanoyl-, Bl-Na-nonanoyl-LysB28, ProB29-human insulin analog. B28-Ne-Nonanoyl-, Al-Na-nonanoyl-LysB28, ProB29-human insulin analog. Al-Na-Nonanoyl-, Bl-Na-nonanoyl-LysB28, ProB29-human insulin analog. B2 8 -Ne-Nonanoyl -, Al -Na-nonanoyl -, Bl -Na- nonanoyl - LysB28,ProB29-human insulin analog. B28-Ne-Decanoyl-LysB28,ProB29-huraan insulin analog. Bl-Na-Decanoyl-LysB28,ProB29-human insulin analog. Al-Na-Decanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Decanoyl-,Bl-Na-decanoyl-LysB28, ProB29-human insulin analog. B28-Ne-Decanoyl-, Al-Na-decanoyl-LysB28, ProB29-human insulin analog. Al-Na-Decanoyl-, Bl-Na-decanoyl-LysB28, ProB29-human insulin analog. B28-Ne-Decanoyl-, Al-Na- decanoyl-, Bl-Na-decanoyl- LysB28,ProB29-human insulin analog. B28-Ne-Undecanoyl-LysB28,ProB29-huroan insulin analog. Bl-Na-Dndecanoyl-LysB28,ProB29-hnBan insulin analog. Al-Na-nDdecanoyl-LysB28(ProB29-lBaBan insulin analog. B28-Ne-Dodecanoyl-LysB28,ProB29-nu»an insulin analog. Bl - Na- Dodecanoyl -LysB2 8, ProB2 9 -human insulin analog Al-Na-Dodecanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Tridecanoyl-LysB28,ProB29-human insulin analog. Bl -Na-Tr idecanoy 1 - Ly sB2 8, ProB29 - hrnna n insulin analog. Al-Na-Tridecanoyl-LysB28,ProB29-human insulin analog. B2 8 -Ne- Tetradecanoy 1 - LysB2 8, ProB2 9 - human insul in anal og. Bl -Na-Tetradecanoyl - LysB2 8, ProB2 9 - human insul in analog. Al-Na-Tetradecanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Pentadecanoyl-LysB28,ProB29-human insulin analog. Bl-Na-Pentadecanoyl-LysB28, ProB29-human insulin analog. Al-Na-Pentadecanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Hexadecanoyl-LysB28,ProB29-human insulin analog. Bl-Na-Hexadecanoyl-LysB28,ProB29-human insulin analog. Al-Na-Hexadecanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Heptadecanoyl-LysB28,ProB29-human insulin analog. Bl-Na-Heptadecanoyl-LysB28,ProB29-human insulin analog. Al-Na-Heptadecanoyl-LysB28,ProB29-human insulin analog. B28-Ne-Octadecanoyl-LysB28,ProB29-human insulin analog. Bl-Na-Octadecanoyl-LysB28,ProB2S-human insulin analog. Al-Na-Octadecanoyl-LysB28,ProB29-human insulin analog. B29-Ne-Pentanoyl-GlyA21,ArgB31,ArgB32-human insulin. Bl-Na-Hexanoyl-GlyA21,ArgB31,ArgB32-human insulin. Al-Na-Heptanoyl -GlyA21, ArgB31, ArgB32 -human insulin. B2 9-Ne-Octanoyl -, Bl-Na- octanoyl - GlyA21, ArgB31, ArgB3 2 - human insulin. B29-Ne-Propionyl-, Al-Na-propionyl-GlyA21, ArgB31, ArgB32-human insulin. Al -Na-Acetyl, Bl -Na- acetyl -GlyA21, ArgB31, ArgB3 2 - human insulin. B2 9 -Ne-Fonnyl -, Al -Na-f ornryl -, Bl -Na- f ormyl - GlyA21, ArgB31, ArgB3 2 - human insul in. B2 9 -Ne-Formyl -des (TyrB26) -human insulin. Bl -Ha- Acetyl -AspB28-human insulin. B29-Ne-Propionyl-, Al-Na-propiccyl-, Bl-Ka-propionyl- AspBlrAspB3,AspB21-human insulin. Al-Na-Butyryl-AspBlO-human insulin. B29-NE-Pentanoyl-GlyA21-human insulin. Bl -Na- Hexanoy 1 - GlyA21 - human insul in. Al-Na-Heptanoyl-GlyA21-human insulin. B29-Ne-Octanoyl-,Bl-Na-octanoyl-GlyA21-human insulin. B29-Ne-Propionyl-, Al-Na-propionyl-GlyA2l-human insulin. Al-Na-Acetyl, Bl-Na-acetyl-GlyA21-human insulin. B29-Ne-Formyl- , Al-Na-f ormyl- , Bl-Na-formyl-GlyA21-human insulin. B29-Ne-Butyryl-des(ThrB3 0) -human insulin. Bl-Na-Butyryl-des(ThrB30)-human insulin. Al-Na-Butyryl-des(ThrB30)-human insulin. B29-Ne-Butyryl-, Bl-Na-butyryl-des (ThrB30) -human insulin. B29-Ne-Butyryl-, Al-Na-butyryl-des (ThrB30) -human insulin. Al-Na-Butyryl-, Bl-Na-butyryl-des (ThrB30) -human insulin. B29-Ne-Butyryl-, Al-Na-butyryl-, Bl-Na-butyryl-des (ThrB30) - human insulin. Aqueous compositions containing water as the major solvent are preferred. Aqueous suspensions wherein water is the solvent are highly preferred. The compositions of the present invention are used to treat patients who have diabetes or hyperglycemia. The formulations of the present invention will typically provide derivatized protein at concentrations of from about 1 mg/mL to about 10 mg/mL. Present formulations of insulin products are typically characterized in terms of the concentration of units of insulin activity (units/mL), such as U40, U50, 0100, and so on, which correspond roughly to about 1.4, 1.75, and 3.5 mg/mL preparations, respectively. The dose, route of administration, and the number of administrations per day will be determined by a physician considering such factors as the therapeutic objectives, the nature and cause of the patient's disease, the patient's gender and weight, level of exercise, eating habits, the Method of administration, and other factors known to the skilled physician. In broad range, a daily dose would be in the range of from about 1 nmol/kg body weight to about 6 nmol/kg body weight (6 nmol is considered equivalent to about 1 unit of insulin activity) . A dose of between about 2 and about 3 nmol/kg is typical of present insulin therapy. The physician of ordinary skill in treating diabetes will be able to select the therapeutically most advantageous means to administer the formulations of the present invention. Parenteral routes of administration are preferred. Typical routes of parenteral administration of suspension formulations of insulin are the subcutaneous and intramuscular routes. The compositions and formulations of the present invention may also be administered by nasal, buccal, pulmonary, or occular routes. Glycerol at a concentration of 12 mg/mL to 25 mg/mL is preferred as an isotonicity agent. Yet more highly preferred for isotonicity is to use glycerol at a concentration of from about 15 mg/mL to about 17 mg/mL. M-cresol and phenol, or mixtures thereof, are preferred preservatives in formulations of the present invention. Insulin, insulin analogs, or proinsulins used to prepare derivatized proteins can be prepared by any of a variety of recognized peptide synthesis techniques including classical (solution) methods, solid phase methods, semi- synthetic methods, and more recent recombinant DNA methods. For example, see Chance, R. E., et al., U.S. Patent No. 5,514,646, 7 May 1996; EPO publication number 383,472, 7 February 1996; Brange, J. J. V., et al. EPO publication number 214,826, 18 March 1987; and Belagaje, R. M. , et a.1., U.S. Patent No. 5,304,473, 19 April 1994, which disclose the preparation of various proinsulin and insulin analogs. These references are expressly incorporated herein by reference. Generally, derivatized proteins are prepared using methods known in the art. The publications listed above to describe derivatized proteins contain suitable methods to prepare derivatized proteins. Those publications are expressly incorporated by reference for methods of preparing derivatized proteins. To prepare acylated proteins, the protein is reacted with an activated organic acid, such as an activated fatty acid. Activated fatty acids are derivatives of commonly employed acylating agents, and include activated esters of fatty acids, fatty acid halides, activated amides of fatty acids, such as, activated azolide derivatives [Hansen, L. B., WIPO Publication No. 98/02460, 22 January 1998], and fatty acid anhydrides. The use of activated esters, especially N-hydroxysuccinimide esters of fatty acids, is a particularly advantageous means of acylating a free amino acid with a fatty acid. Lapidot, et al. describe the preparation of N-hydroxysuccinimide esters and their use in the preparation of N-lauroyl-glycine, N- lauroyl-L-serine, and N-lauroyl-L-glutamic acid. The term "activated fatty acid ester" means a fatty acid which has been activated using general techniques known in the art [Riordan, J- F. and Vallee, B. L., Methods in Enzymology, XXV:494-499 (1972); Lapidot, Y., et al., J. Lipid Res. 8:142-145 (1967)]. Hydroxybenzotriazide (HOBT), N- hydroxysuccinimi.de and derivatives thereof are particularly well known for forming activated acids for peptide synthesis. To selectively acylate the e-amino group, various protecting groups may be used to block the a-amino groups during the coupling. The selection of a suitable protecting group is known to one skilled in the art and includes p- methoxybenzoxycarbonyl (pmZ) . Preferably, the e-amino group is acylated in a one-step synthesis without the use of amino-protecting groups. A process for selective acylation at the Ne-amino group of Lys is disclosed and claimed by Baker, J. C, et al., U.S. Patent No. 5,646,242, 8 July 1997, the entire disclosure of which is incorporated expressly by reference. A process for preparing a dry powder of an acylated protein is disclosed and claimed by Baker, J. C, et al., U.S. Patent No. 5,700,904, 23 December 1997, the entire disclosure of which is incorporated herein expressly by reference. The primary role of zinc in the present invention is to facilitate formation of Zn(II) hexamers of the protein and derivatized protein, either separately as mixed hexamers, or together as hybrid hexamers. Zinc facilitates the formation of hexamers of insulin, and of insulin analogs. Zinc likewise promotes the formation of hexamers of derivatized insulin and insulin analogs. Hexamer formation is conveniently achieved by bringing the pH of a solution comprising protein, or derivatized protein, or both into the neutral region in the presence of Zn{II) ions, or by adding Zn(II) after the pH has been adjusted to the neutral region. For efficient yield of microcrystals or amorphous precipitate, the molar ratio of zinc to total protein in the microcrystal and amorphous precipitate of the present invention is bounded at the lower limit by about 0.33, that is, the approximately two zinc atoms per hexamer which are needed for efficient hexamerization. The microcrystal and amorphous precipitate compositions will form suitably with about 2 to about 4-6 zinc atoms present when no compound that competes with insulin for zinc binding is present. Even more zinc may be used during the process if a compound that competes with the protein for zinc binding, such as one containing citrate or phosphate, is present. Excess zinc above the minimum amount needed for efficient hexamerization may be desirable to more strongly drive hexamerization. Also, excess zinc above the minimum amount can be present in a formulation of the present invention, and may be desirable to improve chemical and physical stability, to improve suspendability, and possibly to further extend time-action. Consequently, there is a fairly wide range of zinc:protein ratios allowable in the insoluble compositions, processes, and formulations of the present invention. In accordance with the present invention, zinc is present in the formulation in an amount of from about 0.3 mole to about 7 moles per mole of total protein and more preferably about from 0.3 mole to about 1.0 mole of total protein. Yet more highly preferred is a ratio of zinc to derivatized protein from about 0.3 to about 0.7 mole of zinc atoms per mole of total protein. Most highly preferred is a ratio of zinc to total protein from about 0.3 0 to about 0.55 mole of zinc atoms per mole of total protein. For higher zinc formulations that are similar to PZI preparations, the zinc ratio is from about 5 to about 7 moles of zinc per mole of total protein. The zinc compound that provides zinc for the present invention may be any pharmaceutically acceptable zinc compound. The addition of zinc to insulin preparations is known in the art, as are pharmaceutically acceptable sources of zinc. Preferred zinc compounds to supply zinc for the present invention include zinc chloride, zinc acetate, zinc citrate, zinc oxide, and zinc nitrate. A complexing compound is required for the microcrystals and precipitates of the present invention. The complexing compound must be present in sufficient quantities to cause substantial precipitation and crystallization of the hexamers. Such quantities can be readily determined for a particular preparation of a particular complexing compound by simple titration experiments. Ideally, the complexing compound concentration is adjusted so that there is negligible complexing compound remaining in the soluble phase after completion of precipitation and crystallization. This requires combining the complexing compound based on an experimentally determined "isophane" ratio. This ratio is expected to be very similar to that of NPH and NPL. However, it may be slightly different because derivatization may affect the nature of the protein-protamine interaction. When protamine is the complexing compound, it is present in the microcrystal in an amount of from about 0.15 mg to about 0.5 mg per 3.5 mg of the total protein. The ratio of protamine to total protein is preferably from about 0.25 to about 0.40 (mg/mg) . More preferably the ratio is from about 0.25 to about 0.38 (mg/mg) . Preferably, protamine is in an amount of 0.05 mg to about 0.2 mg per mg of the total protein, and more preferably, from about 0.05 to about 0.15 milligram of protamine per milligram of total protein. Protamine sulfate is the preferred salt form of protamine for use in the present invention. When protamine sulfate, or other salt form of protamine is used, the mass of it to be used would have to be adjusted with respect to the mass of protamine free base that would be used for the same application by a factor equal to the ratio of the molecular weights of the salt form and protamine. To further extend the time action of the compositions of the present invention or to improve their suspendability, additional protamine and zinc may be added after crystallization. Thus, also within the present invention are formulations having protamine at higher than isophane ratios. For these formulations, the protamine ratio is from 0.25 mg to about 0.5 mg of protamine per mg of total protein. A required component of the raicrocrystals and precipitates of the present invention is a hexamer stabilizing compound. The structures of three hexameric conformations have been characterized in the literature, and are designated T6, T3R3, and R6. In the presence of hexamer stabilizing compound, such as various phenolic compounds, the R6 conformation is stabilized. Therefore, it is highly likely that hexamers are in the R6 conformation, or the T3R3 conformation in the crystals and precipitates produced in the presence of a hexamer stabilizing compound, such as phenol or m-cresol, among others. A wide range of hexamer stabilizing compounds are suitable. They must be present in sufficient proportions with respect to total protein to stabilize the R6 hexamer conformation. To accomplish this, at least 2 or at least 3 moles of hexamer stabilizing compound per hexamer are required for effective hexamer stabilization. Xt is preferred that at least 3 moles of hexamer stabilizing compound per hexamer be present in the microcrystals and precipitates of the present invention. The presence of higher ratios of hexamer stabilizing compound, at least up to 25 to 50-fold higher, in the solution from which the microcrystals and precipitates are prepared will not adversely affect hexamer stabilization. In formulations of the present invention, a preservative may be present, especially if the formulation is intended to be sampled multiple times. As mentioned above, a wide range of suitable preservatives are known. Preferably, the preservative is present in the solution in an amount suitable to provide an antimicrobial effect sufficient to meet pharmacopoeial requirements. Preferred preservatives are the phenolic preservatives, which are enumerated above. Preferred concentrations for the phenolic preservative are from about 2 mg to about 5 mg per milliliter of the aqueous suspension formulation. These concentrations refer to the total mass of phenolic preservatives because mixtures of individual phenolic preservatives are contemplated. Suitable phenolic preservatives include, for example, phenol, m-cresol, and methylparaben. Preferred phenolic compounds are phenol and m-cresol. Mixtures of phenolic compounds, such as phenol and m-cresol, are also contemplated and highly preferred. Examples of mixtures of phenolic compounds are 0.6 mg/mL phenol and 1.6 mg/mL m-cresol, and 0.7 mg/mL phenol and 1.8 mg/mL m-cresol. The microcrystals of the present invention are preferably oblong-shaped, also known as "rod-like", single crystals that are comprised of a protein, a derivatized protein, a divalent cation, and including a complexing compound and a hexamer-stabilizing compound. The mean length of the microcrystals of the present invention preferably is within the range of 1 micron to 40 microns, and more preferably is within the size range of 3 microns to 15 microns. A preferred composition comprises from about 3 mg to about 6 mg of protamine sulfate per 35 mg of total protein, and from about 0.1 to about 0.4 mg zinc per 35 mg of total protein. Another preferred composition comprises from about 10 mg to about 17 mg of protamine sulfate per 35 mg of total protein, and from about 2.0 to about 2.5 mg zinc per 35 mg of total protein. Another preferred composition comprises, per mL, protamine sulfate, 0.34-0.38 mg; zinc, 0.01-0.04 mg; and total protein, 3.2-3.8 mg. Both an un-derivatized protein and a derivatized protein are required for the present co-crystals and amorphous precipitates. The ratio between the masses of these proteins determines the degree of time extension of the preparations. A preferred ratio of the number of moles of the protein to the number of moles of the derivatized protein is between about 1:100 and about 100:1. A further preferred ratio of the number of moles of the protein to the number of moles of the derivatized protein is between about 1:1 and about 100:1. Another preferred ratio of the number of moles of the protein to the number of moles of the derivatized protein is between about 1:1 and about 20:1. Yet other preferred ratios of the number of moles of the protein to the number of moles of the derivatized protein are: between about 2:1 and about 20:1; between about 2:1 and 10:1; between about 2:1 and 5:1; between about 3:1 and 5:1; between 1:1 and 1:20; between 1:1 and 1:10; between about 1:2 and about 1:20; between about 1:2 and 1:10; between about 1:2 and 1:5; between about 1:3 and 1:5; between about 10:1 and about 1:10; between about 9:1 and about 1:9; between about 5:1 and about 1:5; and between about 3:1 and about 1:3. The present invention provides processes for preparing the compositions. Also, the use of the present insoluble compositions to prepare medicaments for controlling blood glucose, and for treating diabetes or hyperglycemia is contemplated. The amorphous precipitates and microcrystals of the present invention can be prepared for use in medicaments, or other uses, by many different processes. In summary, suitable processes are comprised generally of the steps in one of the following sequences: solubilization (if starting with dry material), hexamerization, liomogenization, complexation, precipitation, crystallization, and optionally formulation; or solubilization (if starting with dry material), homogenization, hexamerization, complexation, precipitation, crystallization, and optionally formulation. Solubilization means the dissolution of derivatized protein and protein sufficiently to allow them to form hexamers. Hexamerization refers to the process wherein molecules of protein and derivatized protein bind with zinc(II) atoms to form hexamers. Complexation denotes the formation of insoluble complexes between the hexamers and protamine. Precipitation results typically from the formation of insoluble complexes. Crystallization involves the conversion of precipitated hexamer/protamine complexes into crystals, typically, rod-like crystals. Solubilization is carried out by dissolving the derivatized protein and protein in an aqueous solvent. The aqueous solvent may be, for example, an acidic solution, a neutral solution, or a basic solution. The aqueous solvent may be comprised partially of a miscible organic solvent, such as ethanol, acetonitrile, dimethyl sulfoxide, and the like. Acidic solutions may be, for example, solutions of HC1, advantageously from about 0.01 N HCl to about 1.0 N HC1. Other acids that are pharmaceutically acceptable may be employed as well. Basic solutions may be, for example, solutions of NaOH, advantageously from about 0.01 N NaOH to about 1.0 N NaOH, or higher. Other bases that are pharmaceutically acceptable may be employed as well. For the sake of protein stability, the con centra t ion of acid or base is preferably as low as possible while still being effective to adequately dissolve the protein and derivatized protein. Most proteins (insulin, insulin analogs, and proinsulins) and many derivatized proteins may be dissolved to suitable concentrations at neutral pH. Solutions to dissolve derivatized proteins at neutral pH may contain a buffer and optionally, one or more additional solutes such as salts, phenolic compounds, zinc, and isotonicity agents. When hexamerization occurs before homogenization, two populations of homogenous hexamers are formed first, and then the populations are mixed, thereby forming mixed hexamers. When homogenization occurs first, hexamerization yields hybrid hexamers. As mentioned above, to prepare insoluble compositions comprised of hybrid hexamers, protein and derivatized protein are homogenized under conditions favoring dissociation to monomer or dimer aggregation states prior to hexamerization with a divalent metal cation. To achieve the necessary dissociation, the protein and derivatized protein may be mixed under strongly acidic or strongly basic conditions. The degree of dissociation, and therefore, homogenization is influenced by the solution conditions chosen for this step. Insulin and related proteins readily self-associate in a series of reactions producing dimers, hexamers, and other associated forms. The distribution of these association forms at equilibrium is dependent on many parameters, including pH. These association reactions are commonly thought to involve primarily monomer-dimer-hexamer assembly. Consequently, depending on the solution conditions chosen, homogenization should accomplish the mixing of monomers, dimers, or a mixture thereof. Homogenization in 1 N HC1, for example, could involve a higher fraction of monomer mixing than in 0.1 N HC1, which would probably involve more dimer mixing. For the preparation of compositions comprised of hybrid hexamers, the homogenization process will be effective provided that only a very small or negligible fraction of homogeneous hexamers of the protein or derivatized protein exist under the homogenization conditions employed. Compositions comprised of mixed hexamers incorporate predominantly two types of hexamers, namely hexamers of the protein, and hexamers of the derivatized protein. In this case, the homogenization step occurs after the hexamerization step, and achieves the homogenization of the hexamers prior to complexation with the complexing compound. Consequently, the homogenization step is performed under solution conditions that stabilize the Zn(II)-insulin hexamer. Solution conditions that stabilize insulin hexamers are well known in the literature. The solution conditions required for hexamerization are those that allow the formation of the hybrid hexamers or mixed hexamers in solution. These conditions will be identical or very similar to the conditions under which insulin or insulin analogs are made to hexamerize. Typically, hexamerization requires zinc and a neutral to slightly basic pH, which is taken to be from about pH 6.8 to about pH 8.4. The presence of a hexamer- stabilizing compound advantageously influences hexamerization by promoting the R6 or the T3R3 conformations of the derivatized protein, and in certain instances, of the protein also. For certain monomeric insulin analogs, a hexamer-stabilizing compound is required to form hexamers. For compositions comprised of hybrid hexamers, seven hexameric species are expected: P6, P2D1 P4D2, P3D3, P2D4, P2D5, and D6, where P represents the protein monomer, and D represents the derivatized protein monomer. The statistical distribution of hexamers is expected to conform to a Poisson distribution, and will be influenced by the relative proportion of protein and derivatized protein, and by the degree of dissociation prior to hexamerization. For example, from a homogenized solution constituted predominantly of dimers, four major hybrid hexamer species are expected: P6, P4D2, P2D4, and D6. For compositions comprised of mixed hexamers, only two hexameric species are expected to predominate: P6 and D6. The complexation step must involve the combination a complexing compound with hexamer under solution conditions where each is initially soluble. This could be accomplished by combining separate solutions of hexamers and of protamine, or by first forming a solution of protein, derivatized protein, and protamine at acidic or basic pH, and then shifting the pH to the neutral range. During crystallization, the solution conditions must stabilize the crystallizing species, and promote the conversion of precipitate to solute to crystal. Thus, the solution conditions will determine the rate and outcome of crystallization. Crystallization likely involves a complex equilibrium involving non-crystalline precipitate, dissolved hexamer-protamine complexes, and crystal. To obtain microcrystals, the conditions chosen for crystallization must drive the equilibrium toward crystal formation. Also, in light of the hypothesized equilibrium, the solubility of the derivatized protein is expected to profoundly affect crystallization rate and size because lower solubility will likely slow the net conversion from precipitate to solution to crystal. Furthermore, it is well-recognized that slowing the rate of crystallization often results in larger crystals. Thus, the crystallization rate and crystal size are thought to depend on the size and nature of the derivatizing moiety on the derivatized protein. Crystallization parameters that influence the crystallization rate and the size of crystals of the present invention are: acyl group size and nature; temperature; the presence and concentration of compounds that compete with the protein and derivatized protein for zinc, such as citrate, phosphate, and the like; the nature and concentration of phenolic compound (s); zinc concentration; the presence and concentration of a miscible organic solvent; the time permitted for crystallization; the pH and ionic strength; buffer identity and concentration; the concentration of precipitants; the presence of seeding materials; the shape and material of the container; the stirring rate; and the total protein concentration. Temperature and the concentration of competing compounds are thought to be of particular importance. Competing compounds, such as citrate, may affect the rate at which crystals form, and indirectly, crystal size and quality. These compounds may exert their effect by forming coordination complexes with zinc in solution, thus competing with the relatively weak zinc binding sites on the surface of the hexamer for zinc. Occupation of these weak surface binding sites probably impedes crystallization. Additionally, many derivatized proteins are partially insoluble in the presence of little more than 0.333 zinc per mole of derivatized protein, and the presence of competing compounds restores solubility, and permits crystallization. The optimum concentration of competing compound can be determined using routine techniques for any combination of protein and derivatized protein. As an upper limit, of course, is the concentration at which zinc is precipitated by the competing compound, or the concentration at which residual competing compound would be pharmaceutically unacceptable, such as, when it would cause pain or irritation at the site of administration. An example of a process for preparing the precipitates and crystals of the present invention follows. A measured amount of the derivatized protein and a measured amount of the protein are dissolved in, or are combined to form a solution in an aqueous solvent containing a hexamer- stabilizing compound, such as a phenolic compound. To this solution is added a solution of zinc as one of its soluble salts, for example Zn(II)Cl2, to provide from about 0.3 moles of zinc per mole of derivatized insulin to about 0.7 moles, or to as much as 1.0 moles, of zinc per mole of total protein (protein + derivatized protein). Absolute ethanol, or another miscible organic solvent, may optionally be added to this solution in an amount to make the solution from about 5% to about 10% by volume organic solvent. This solution may then be filtered through a 0.22 micron, low- protein binding filter. A protamine solution is prepared by dissolving a measured amount of protamine in an aqueous solvent. This solution may be filtered through a 0.22 micron, low-protein binding filter. The solution of protein and derivatized protein and the protamine solution are combined, whereupon a precipitate forms initially. The resulting suspension is stirred slowly at room temperature (typically about 20-25°C), whereupon microcrystals are formed within a period from about 4 hours to about 10 days. The microcrystals may then be separated from the mother liquor and introduced into a different solvent, for storage and administration to a patient. Examples of appropriate aqueous solvents are as follows: water for injection containing 25 mM TRIS, 5 mg/mL phenol and 16 mg/mL glycerol; water for injection containing 2 mg/mL sodium phosphate dibasic, 1.6 mg/mL m-cresol, 0.65 mg/mL phenol, and 16 mg/mL glycerol; and water for injection containing 25 mM TRIS, 5 mg/mL phenol, 0.1 M trisodium citrate, and 16 mg/mL glycerol. In another process for preparing the insoluble compositions of the present invention, for example, a measured mass of dry derivatized protein and a measured mass of dry protein are dissolved together in an acidic aqueous solvent, such as 0.1 N - 1.0 N HC1. This solution is stirred to insure thorough mixing of derivatized protein and protein. The ratio of derivatized protein powder to protein powder in this mixture is predefined to achieve a similar ratio of derivatized protein to protein in the insoluble composition to be produced. A separately prepared aqueous solution comprised of a phenolic preservative and, optionally, a pharmaceutically acceptable buffer, is combined with the acidic solution of the proteins. The pH of the resulting solution is then adjusted to about 6.8 to about 8.4, preferably from about 6.8 to about 8.0, or preferably to a pH of from about 7.2 to about 7.8, and most preferably from about 7.4 to about 7.8. To this solution is added a solution of zinc as one of its soluble salts, for example Zn(II)Cl2, to provide from about 0.3 moles of zinc per mole of total insulin to about 4 moles of zinc per mole of total insulin. This solution is adjusted to a pH as given above, and preferably to about 7.4 -7.6, and may then be filtered through a 0.22 micron, low-protein binding filter. A solution of protamine is prepared by dissolving a measured mass of protamine in an aqueous solvent. The protamine solution may be filtered through a 0.22 micron, low-protein binding filter. The solution of protein and derivatized protein and the protamine solution are combined, whereupon a precipitate forms initially. The resulting suspension is stirred slowly at room temperature (typically about 20-25°C), whereupon microcrystals are formed within a period from about 4 hours to about 10 days. In another process for preparing the insoluble compositions of the present invention, a measured amount of a derivatized protein is first dissolved in an aqueous solvent containing a phenolic preservative. To this solution is added a solution of zinc as one of its soluble salts, for example Zn{II)Cl2, to provide from about 0.3 moles of zinc per mole of derivatized protein to about 4 moles of zinc per mole of derivatized protein. The pH of the resulting solution is then adjusted to about 6.8 to about 8.4, preferably from about 6.8 to about 8.0, or preferably to a pH of from about 7.2 to about 7.8, and most preferably from about 7.4 to about 7.8. A second solution is prepared separately wherein a measured amount of a protein selected from the group consisting of insulin, insulin analogs, and proinsulin is dissolved in an aqueous solvent containing a phenolic preservative. To this solution is added a solution of zinc as one of its soluble salts, for example Zn(II)Cl2, to provide from about 0.3 moles of zinc per mole of protein to about 4 moles of zinc per mole of protein. The pH of the resulting solution is then adjusted to about 6.8 to about 8.4, preferably from about 6.8 to about 8.0, or preferably to a pH of from about 7.2 to about 7.8, and most preferably from about 7.4 to about 7.8, or 7.4 - 7.6. Portions of the derivatized protein solution and the protein solution are combined in a ratio that is predefined in order to achieve a similar ratio of derivatized protein to protein in the insoluble composition. This solution is stirred to insure thorough mixing of derivatized protein and protein. This solution is then adjusted to a pH of about 7.6, and may then be filtered through a 0.22 micron, low-protein binding filter. A protamine solution is prepared separately by dissolving a measured amount of protamine in an aqueous solvent. This protamine solution may be filtered through a 0.22 micron, low-protein binding filter. The solution of protein and derivatized protein and the protamine solution are combined, whereupon a precipitate forms initially. The resulting suspension is stirred slowly at room temperature (typically about 20-25"0, whereupon microcrystals are formed within a period from about 4 hours to about 10 days. While not describing all of the very many types of processes that will produce the insoluble compositions of the present invention in any way, the following are yet further processes of the present invention: dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers, and adding a complexing compound; dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will not permit the formation of hexamers, adjusting the pH to between about 6.8 and about 7.8, and adding a complexing compound; dissolving a protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers, separately, dissolving a derivatized protein, a hexamer- stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers, thoroughly mixing together these two solution, and then adding a complexing compound; dissolving a protein, a hexamer-stabilizing compound, a divalent metal cation, and a complexing compound in an aqueous solvent, wherein the resulting solution has a pH at which precipitation does not occur, separately, dissolving a derivatized protein, a hexamer-stabilizing compound, a divalent metal cation, and a complexing compound in an aqueous solvent, wherein the resulting solution has a pH at which precipitation does not occur, thoroughly mixing together these two solutions, and adjusting the pH of the solution of to a value at which precipitation occurs; dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, a divalent metal cation, and a complexing compound in an aqueous solvent, wherein the resulting solution has a pH at which precipitation does not occur and adjusting the pH of the solution to a value at which precipitation occurs; dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation, in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing agent is added, adding a complexing compound, and adjusting the pH of the solution of step b) to a value at which precipitation occurs; dissolving a protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added, separately, dissolving a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added, thoroughly mixing together these two solutions, adding complexing compound together solution, and adjusting the pH to a value at which precipitation occurs; dissolving a protein, a protein derivative, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added, adjusting the pH of the solution to a value at which precipitation will occur when a complexing compound is added, and adding a complexing compound to the solution; dissolving a protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added, separately, dissolving a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added; thoroughly mixing together these two solutions, adjusting the pH of the solution of step c) to a value at which precipitation will occur when a complexing compound is added, and adding a complexing compound to the solution; In a preferred embodiment, the microcrystals are prepared in a manner that obviates the need to separate the microcrystals from the mother liquor. Thus, it is preferred that the mother liquor itself be suitable for administration to the patient, or that the mother liquor can be made suitable for administration by dilution with a suitable diluent. The terra diluent will be understood to mean a solution comprised of an aqueous solvent in which is dissolved various pharmaceutically acceptable excipients, including without limitation, a buffer, an isotonicity agent, zinc, a preservative, protamine, and the like. In addition to the protein, derivatized protein, divalent cation, complexing compound, and hexamer- stabilizing compound, pharmaceutical compositions adapted for parenteral administration in accordance with the present invention may employ additional excipients and carriers such as water miscible organic solvents such as glycerol, sesame oil, aqueous propylene glycol and the like. When present, such agents are usually used in an amount less than about 2.0% by weight based upon the final formulation. For further information on the variety of techniques using conventional excipients or carriers for parenteral products, please see Remington's Pharmaceutical Sciences, 17th Edition, Mack Publishing Company, Easton, PA, USA (1985), which is incorporated herein by reference. In the broad practice of the present invention, it is also contemplated that a formulation may contain a mixture of the microcrystals and a soluble fraction of a protein selected from insulin, derivatized insulin, insulin analogs, and derivatized insulin analogs. Examples of such pharmaceutical compositions include sterile, isotonic, aqueous saline solutions of insulin, an insulin analog, a derivatized insulin, or a derivatized insulin analog, buffered with a pharmaceutically acceptable buffer and pyrogen-free. Preferred for the soluble phase are insulin or a rapidr-acting insulin analog" such as, LysB28,ProB29- human insulin, or AspB28-human insulin. Such mixtures are designed to provide a combination of meal-time control of glucose levels, which is provided by the soluble insulin, and basal control of glucose levels, which is provided by the insoluble insulin. The ratio of total protein (protein plus derivatized protein) in the insoluble phase and total protein in the soluble phase is in the range of about 9:1 to about 1:9. A preferred range of this ratio is from about 9:1 to about 1:1, and more preferably, about 7:3. Other ratios are 1:1, and 3:7. The following preparations and examples illustrate and explain the invention. The scope of the invention is not limited to these preparations and examples. Reference to "parts" for solids means parts by weight. Reference to "parts" for liquids means parts by volume. Percentages, when used to express concentration, mean mass per volume (x100). All temperatures are degrees Centigrade (°C) . "TRIS" refers to 2-amino-2-hydroxymethyl-l,3,-propanediol. The 1000 part-per-million (ppm) zinc solution was prepared by diluting 1.00 mL of a 10,000 ppm zinc atomic absorption standard solution [Ricca Chemical Company, zinc in dilute nitric acid] with water to a final volume of 10.00 mL. In many of the preparations described below, the yield of precipitates and crystals was estimated. The yield estimate relied on determination of the amount of total protein in the precipitate or crystal, and on an estimate of the amount of the same initially in solution. To determine the amount of total protein, samples of re-dissolved precipitate or crystal, and of the supernatant above the precipitate or crystals, were analyzed by reversed-phase gradient HPLC, as described below. Briefly, the analytical system relied on a C8 reversed-phase column, at 23°C. The flow rate was 1.0 roL/min and UV detection at 214 nm was used. Solvent A was 0.1% (vol:vol) trifluroacetic acid in 10:90 (vol:vol) acetonitrile:water. Solvent B was 0.1% (vol:vol) trifluroacetic acid in 90:10 (vol:vol) acetonitrile:water. The development program was (minutes, %B) : (0.1,0); (45.1,75); (50.1,100); (55,100); (57,0); (72,0). All changes were linear. Other analytical systems could be devised by the skilled person to achieve the same objective. To prepare for the HPLC analysis, aliguots of the well-mixed suspensions were dissolved by diluting with either 0.01 N HC1 or 0.03 N HC1. Results of HPLC analysis of these solutions permitted calculation of total protein. Aliguots of the suspensions were centrifuged for approximately 5 minutes in an Eppendorf 5415C microcentrifuge at 14,000 rpm. The decanted supernatant was diluted with either 0.01 If or 0.1 N HC1 and analyzed by HPLC. The precipitate was washed by re-suspending in Dulbecco's phosphate buffered saline (without calcium or magnesium) and re-pelleted by centrifugation. The buffer was decanted and the solid was re-dissolved in 0.01 N HC1. The re-dissolved precipitate was analyzed by HPLC. HPLC was used to confirm the presence of the expected proteins in the acidified suspension, re-dissolved precipitate, and supernatant and also to determine protein concentrations. The retention times of peaks in the chromatograms of the re-dissolved precipitates were compared with the retention times observed for protamine and the active compounds used to make the formulations. The agreement between retention times was always good, showing that protamine, protein, and derivatized proteins were actually incorporated into the microcrystals. Concentrations of protein and derivatized protein were determined by comparing the appropriate peak areas to the areas of a standard. A 0.22 mg/mL solution of derivatized insulin was used as the standard. A standard containing protamine was run, but only for the purpose of determining the retention time. Protamine concentration was not quantitated. In many of the preparations described below, a standard spectrophotometry assay was used to determine how rapidly the crystals dissolved in Dulbecco's phosphate buffered saline (pH 7.4) at room temperature. Significant deviations from the procedure described immediately below are noted where appropriate in the descriptions of the preparations. A spectrophotometer suitable for measuring in the ultraviolet range, and equipped with a l cm cuvette and a magnetic cuvette stirrer was used for all the dissolution assays. The cuvette, containing a small stir bar and 3.00 mL of phosphate buffered saline (PBS), was put into the cell compartment of the spectrophotometer. The instrument was set to 320 nm and zeroed against the same buffer. Then 4.0 microliters of a well suspended formulation, usually having a total concentration approximately equivalent to a U50 formulation, or about 1.6 to 1.8 mg/mL, was added to the cuvette. After waiting 1.0 minute for mixing, the optical density at 320 nm was recorded. Since the proteins involved in this work do not absorb light at 320 nm, the decrease in optical density was due to reduction in light scattering as the crystals dissolved. The time for the optical density to drop to half of its initial value is typically reported (tl/2). As a control, 2.0 microliters of U100 Humulin® N (i.e., human insulin NPH, which is also known as human NPH insulin) was added to 3.00 mL of PBS buffer, and the optical density at 320 nm monitored as above. The dissolution half- time (tl/2) for the Humulin® N formulation was about 6 minutes. Preparation 1 9:1 co-crystals of human insulin and B29-Ne-oetanoyl- human insulin A dry powder of B29-NE-octanoyl-LysB29 human insulin (0.7 parts by mass) and a dry powder of human insulin (6.3 parts by mass) are dissolved in 1000 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 75 parts of a 15.3 mM solution of zinc chloride. The pH is adjusted to 7.6 with 1 N HC1 and/or 1 N NaOH. This solution is filtered through a 0.22 micron, low- protein binding filter. A second solution is prepared by dissolving 7 parts by mass of protamine sulfate in 10,000 parts by volume of water then filtering through a 0.22 micron, low-protein binding filter. Equal volumes of the solution containing insulin and acylated insulin and of the protamine sulfate solution are combined. Initially, an amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate converts to a co- crystalline microcrystalline solid. Preparation 2 3:1 co-crystals of human insulin and B29-Ne-octanoyl- human insulin The procedure of Preparation 1 is followed, except that 1.75 parts by mass of a dry powder of E29-Ne-octanoyl- LysB29 human insulin and 5.25 parts by mass of a dry powder of human insulin are used. After equal volumes of the solution containing insulin and acylated insulin and of the protamine sulfate solution are combined, an amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate converts to a co-crystalline microcrystalline solid. Preparation 3 Formulation of 3:1 co-crystals of human insulin and B29-Ne- octanoyl-human insulin The co-crystalline microcrystals prepared by the method of Preparation 1 are separated from the supernatant and are recovered by conventional solid/liquid separation methods, such as, filtration, centrifugation, or decantation. The recovered co-crystalline microcrystals are then suspended in a solution consisting of 25 mM TRIS, 5 mg/ml phenol, and 16 mg/ml glycerol, pH 7.8, so that the final concentration of insulin activity is about 100 U/mL. Preparation 4 1:1 co-crystals of human insulin and B29-Ne-octanoyl- human insulin The procedure of Preparation 1 is followed, except that 3.5 parts by mass of a dry powder of B29-Ne-octanoyl- LysB29 human insulin and 3.5 parts by mass of a dry powder of human insulin are used. After equal volumes of the solution containing insulin and acylated insulin and of the protamine sulfate solution are combined, an amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate converts to a co-crystalline microcrystalline solid. Preparation 5 1:3 co-crystals of human insulin and B29-Ne-octanoyl- human insulin The procedure of Preparation 1 is followed, except that 5.25 parts by mass of a dry powder of B29-Ne-octanoyl- LysB29 human insulin and 1.75 parts by mass of a dry powder of human insulin are used. After equal volumes of the solution containing insulin and acylated insulin and of the protamine sulfate solution are combined, an amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate converts to a co-crystalline microcrystalline solid. Preparation 6 3:1 co-crystals of human insulin and B29-Ne-hexanoyl- human insulin The procedure of Preparation 1 is followed, except that 1.75 parts by mass of a dry powder of B29-Ne-hexanoyl- LysB29 human insulin and 5.25 parts by mass of a dry powder of human insulin are used. After equal volumes of the solution containing insulin and acylated insulin and of the protamine sulfate solution are combined, an amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate will convert to a co-crystalline microcrystalline solid. Preparation 7 3:1 co-crystals of human insulin and B29-Ne-butyxl-human insulin The procedure of Preparation 1 is followed, except that 1.75 parts by mass of a dry powder of B29-Ne-butyryl- LysB29 human insulin and 5.25 parts by mass of a dry powder of human insulin are used. After equal volumes of the solution containing insulin and acylated insulin and of the protamine sulfate solution are combined, an amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate will convert to a co-crystal line microcrystalline solid. Preparation 8 Co-crystalline microcrystals of protamine-zinc- B29-Ne-octanoyl-hunan insulin-human insulin B29-Ne-octanoyl-LysB29 human insulin (20.1 mg) was dissolved in 1 nL of a solvent composed of 0.1 N HC1. Human insulin (19.3 mg) was dissolved in 1 mL of a solvent composed of 0.1 N HC1. Five solutions comprising different ratios of B29-Ne-octanoyl-LysB29 human insulin to human insulin were prepared by combining volumes of each solution in the ratios shown below. To each of these five solutions, 1.6 mL of a solvent composed of 50 mM TRIS buffer, 0.1 M trisodium citrate, and 10 mg/mL phenol at pH 7.6 was added. To each of the five solutions, 0.15 ml of a 15.3 mM solution of zinc chloride was added. Each of the resulting five solutions were adjusted to a pH of 7.6 with 1 N NaOH. Each of the resulting five solutions were filtered through a 0.22 micron, low-protein binding filter. An additional solution was prepared by dissolving 3.50 mg of protamine sulfate in 10 mL of water then filtered through a 0.22 micron, low- protein binding filter. A volume of 1.9 mL of each of the five solutions and 1.9 mL of the protamine sulfate solution were combined respectively, in each of the five solutions resulting in the immediate appearance of an amorphous precipitate. These five solutions were allowed to stand for 24 hours at room temperature (approximately 22°C) . This procedure resulted in the formation of a white-to-off-white microcrystalline solid in each of the five solutions. Preparation 9 9:1 co-crystals of human insulin and B29-Ne-octanoyl- human insulin A dry powder of B29-Ne-octanoyl-LysB29 human insulin (0.7 parts by mass) is dissolved in 100 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 7.5 parts of a 15.3 mM solution of zinc chloride. A second solution is prepared wherein a dry powder of human insulin (6.3 parts by mass) is dissolved in 900 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 67.5 parts of a 15.3 mM solution of zinc chloride. The acylated insulin solution and the insulin solution are combined together and stirred to insure mixing of the two solutions. This solution is filtered through a 0.22 micron, low-protein binding filter. A protamine solution is prepared by dissolving 7 parts by mass of protamine sulfate in 10,000 parts by volume of water then filtering through a 0.22 micron, low-protein binding filter. Equal volumes of the acylated insulin solution and of the protamine sulfate solution are combined. An amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate will convert to a co-crystalline raicrocrystalline solid. Preparation 10 3:1 co-crystals of buan insulin and B29-Ne-octanoyl- human insulin A dry powder of B29-Ne-octanoyl-LysB29 human insulin (1.75 parts by mass) is dissolved in 250 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 18.75 parts of a 15.3 mM solution of zinc chloride. A second solution is prepared wherein a dry powder of human insulin (5.25 parts by mass) is dissolved in 750 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 56.25 parts of a 15.3 mM solution of zinc chloride. The acylated insulin solution and the insulin solution are combined together and stirred to insure mixing of the two solutions. This solution is filtered through a 0.22 micron, low-protein binding filter. A protamine solution is prepared by dissolving 7 parts by mass of protamine sulfate in 10,000 parts by volume of water then filtering through a 0.22 micron, low-protein binding filter. Equal volumes of the acylated insulin solution and of the protamine sulfate solution are combined. An amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate converts to a co- crystalline microcrystalline solid. Preparation 11 1:1 co-crystal" of human insulin and B29-Ne-octanoyl- human insulin A dry powder of B29-Ne-octanoyl-LysB29 human insulin (3.5 parts by mass) is dissolved in 500 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 1.75 parts of a 15.3 mM solution of zinc chloride. A second solution is prepared wherein a dry powder of human insulin (3.5 parts by mass) is dissolved in 500 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 37.5 parts of a 15.3 mM solution of zinc chloride. The acylated insulin solution and the insulin solution are combined together and stirred to insure mixing of the two solutions. This solution is filtered through a 0.22 micron, low-protein binding filter. A protamine solution is prepared by dissolving 7 parts by mass of protamine sulfate in 10,000 parts by volume of water then filtering through a 0.-22 micron, low-protein binding filter. Equal volumes of the acylated insulin solution and of the protamine sulfate solution are combined. An amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22°C) . The amorphous precipitate converts to a co- crystalline microcrystalline solid. Preparation 12 1:3 co-crystals of human, insulin and B29-Ne-octanoyl- human insulin A dry powder of B29-Ne-octanoyl-LysB29 human insulin (5.25 parts by mass) is dissolved in 750 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 56.25 parts of a 15.3 mM solution of zinc chloride. A second solution is prepared wherein a dry powder of human insulin (1.75 parts by mass) is dissolved in 250 parts by volume of an aqueous solvent composed of 50 mM TRIS, 0.1 M trisodium citrate, and 10 mg/ml phenol at pH 7.6. To this solution is added 18.75 parts of a 15.3 mM solution of zinc chloride. The acylated insulin solution and the insulin solution are combined together and stirred to insure mixing of the two solutions. This solution is filtered through a 0.22 micron, low-protein binding filter. A protamine solution is prepared by dissolving 7 parts by mass of protamine sulfate in 10,000 parts by volume of water then filtering through a 0.22 micron, low-protein binding filter. Equal volumes of the acylated insulin solution and of the protamine sulfate solution are combined. An amorphous precipitate forms. This suspension is allowed to stand for about 24 hours at room temperature (typically about 22 °C) . The amorphous precipitate converts to a co- crystalline microcrystalline solid. Preparation 13 Co-crystals of human insulin and B29-Ne-hexanoyl-human insulin An acidic solution of B29-Ne-hexanoyl-human insulin was prepared by dissolving 12.3 mg of B29-Ne- hexanoyl-human insulin in 0.3 mL of 0.1 N HCl. An acidic solution of human insulin was prepared by dissolving 4.6 mg of human insulin (zinc crystals) in 0.1 mL of 0.1 N HC1. The two solutions were combined giving a total volume of 0.4 mL. This resulting solution was stirred for approximately 5 minutes. To this resulting solution was added, with stirring, 0.150 mL of a 1000 ppm zinc(II) solution. A crystallization diluent was prepared comprising 32 mg/mL glycerol, 50 mM tris buffer, 10 mg/mL phenol, 100 mM trisodium citrate, at a pH of 7.6. To the insulin solution was added 1.6 mL of the crystallization diluent. The pH of the solution was adjusted to 7.59 using 1 N NaOH and 1 N HCl. The solution was filtered through a 0.22 micron, low protein binding filter. A protamine solution was prepared by dissolving 7.47 mg of protamine sulfate in 10 mL of water. Two milliliters (2 mL) of the protamine solution was added to 2 mL of the insulin solution. The resulting solution was allowed to stand undisturbed for 18 hours at a controlled temperature of 25°C. Microscopic inspection (at 18 hours) revealed that crystallization had occurred and that the preparation yielded uniform, single, rod-like crystals possessing approximate average lengths of 3 microns. Four milliliters (4 mL) of the crystal formulation produced above after 18 hours were allowed to stand undisturbed overnight, and the crystals sedimented completely. The supernatant was then removed, and replaced with 4 mL of a diluent comprising 16 mg/mL glycerol, 20 mM tris buffer, 1.6 mg/mL m-cresol, 0.65 mg/mL phenol, 40 mM trisodium citrate, pH 7.6. The crystals were then resuspended, and allowed to sediment again. This procedure was carried out three times except that on the third occasion the supernatant was replaced with only 3 mL of diluent. The dissolution rate of the crystals was measured by placing 0.005 mL of the uniformly suspended formulation into 3 mL of Dulbecco's phosphate buffered saline (without calcium or magnesium) in a 1 cm path length square quartz cuvette at a temperature of 22°C. This solution was stirred at a constant rate using a magnetic cuvette stirrer. Absorbance measurements at 320 nm were taken at 1 minute intervals. The absorbance at 320 nm corresponds to the light scattered by the insoluble particles present in the aqueous suspension. Consequently, as the microcrystals dissolve, the absorbance approaches zero. The time required for the 0.005 mL of this formulation to dissolve was greater than 150 minutes. The time required for dissolution of a 0.005 mL sample of D100 commercial Humulin N to dissolve when subjected to the same conditions was about 10 minutes. The amount of total protein in the formulation was analyzed by HPLC to quantitate the total potency. The total potency refers to the total concentration of human insulin and B29-Ne-hexanoyl-human insulin. An aliquot (0.050 mL) of the fully resuspended formulation was dissolved in 0.950 mL of 0.01 N HCL, and subjected to HPLC analysis, as described below. The total potency determined from this analysis was 4.54 mg/mL. For HPLC analyses, the following conditions were used: a C8-reversed phase column; constant 23°C; 1.0 mL/min, detection at 214 nm; solvent A-10% acetonitrile (vol/vol) in 0.1% aqueous trifluoroacetic acid; solvent B=90% acetonitrile (vol/vol) in 0.1% aqueous trifluoroacetic acid; linear gradients (0.1 min, 0%B; 45.1 min, 75%B; 50.1 min, 100%B; 55 min 100%B; 57 min, 0%B; 72 min, 0%B) . Standards were prepared by dissolving bulk insulin and bulk acyl insulin in 0.01 N HCl. The concentration of each standard was determined by UV spectroscopy. A solution of 1.0 mg/ml of human insulin in a 1 cm cuvette was assumed to have an absorbance of 1.0S optical density units at the wavelength maximum (approximately 276 nm) . This corresponds to a molar extinction coefficient of 6098. Acylated insulins were assumed to have the same molar extinction coefficient as human insulin. The solutions calibrated by DV were then diluted to get standards at 0.220, 0.147, 0.073, and 0.022 mg/mL. The standards were run on HPLC and a standard curve of area vs. concentration was obtained. The supernatant was analyzed to determine the total concentration of soluble human insulin and B29-Ne- hexanoyl-human insulin present in the formulation. To 0.040 mL of the supernatant, were added 0.160 mL of 0.01 N HC1. The acidified supernatant was analyzed by HPLC, as described above. The concentration of soluble human insulin and B29- Ne-hexanoyl-human insulin in the supernatant was determined to be 0.07 mg/mL. The ratios of B29-Ne-hexanoyl-human insulin and human insulin in the crystal were determined by sedimenting an aliquot (0.100 mL) of the formulation using a bench-top centrifuge, decanting the supernatant, resuspending the crystals in 0.400 mL of Dulbecco's phosphate-buffered saline, recentrifuging, removing the supernatant, and finally dissolving the crystals in 1.50 mL of 0.01 N HC1. The HPLC analysis described above was performed. The result of this analysis was 64.2% B29-Ne-hexanoyl-human insulin and 15.8% human insulin. Preparation 14 Co-crystal suspension formulation comprising human insulin and B29-lfe-decanoyl-human insulin An acidic solution of B29-Ne-decanoyl-human insulin was prepared by dissolving 10.4 mg of B29-Ne- decanoyl-human insulin in 0.25 mL of 0.1 N HC1. An acidic solution of human insulin was prepared by dissolving M.3 ng of human insulin (zinc crystals) in 0.75 mL of 0.1 N HC1. The two solutions were combined, giving a total volume of 1 mL. This resulting solution was stirred for approximately 5 minutes. To this solution was added, with stirring, 0.305 mL of a 1000 ppm zinc(II) solution. To the resulting solution, was added 4 mL of a crystallization diluent (40 mg/mL glycerol, 50 mM tris buffer, 4 mg/mL m-cresol, 1.625 mg/mL phenol, 100 mM trisodium citrate, pH 7.4) . The pH of the resulting solution was adjusted to 7.58. This solution was filtered through a 0.22 micron, low protein binding filter. Five milliliters (5 mL) of protamine solution (37.6 mg of protamine sulfate in 50 mL of water) was added to 5 mL of the filtered solution. The resulting solution was allowed to stand undisturbed for 63 hours at a controlled temperature of 25°C. Microscopic inspection (at 63 hours) revealed that crystallization had occurred, and that the preparation had yielded uniform, single, rod-like crystals possessing approximate average lengths of 8 microns. The dissolution rate of the crystals was measured by placing 0.006 mL of the uniformly suspended crystal formulation into 3 mL of Dulbecco's phosphate buffered saline (without calcium or magnesium) in a 1 cm path length square quartz cuvette at a temperature of 22°C. The time required for the 0.006 mL of this crystal formulation to dissolve was greater than 300 minutes. The time required for a 0.005 mL sample of 0100 commercial Humulin N to dissolve under the same conditions was about 10 minutes. To prepare for HPLC analysis, the crystals were sedimented by allowing the formulation to stand undisturbed. Eight milliliters (8 mL) of the supernatant were then removed, and were replaced with 8 mL of a diluent [16 mg/mL glycerol, 20 mM tris buffer, 1.6 mg/mL m-cresol, 0.65 mg/mL phenol, 40 mM trisodium citrate, pH 7.6]. The co-crystals were then resuspended. This procedure was carried out in the same way three times, except that on the third occasion, the 8 mL of supernatant was replaced with 7 mL of diluent. Potency of the crystal formulation, and in the supernatant, was analyzed by HPLC, essentially as described in Preparation 13. The total potency determined from this analysis was 3.87 mg/mL. The concentration of soluble human insulin and B29-Ne-decanoyl-human insulin in the supernatant was determined to be 0.06 mg/mL. The proportions of human insulin and B29-Ne-decanoyl-human insulin in the crystal phase were determined by the procedure of Preparation 13 to be 74.3% human insulin, and 25.7% B29-Ne-decanoyl-human insulin. A particle sizing measurement was performed on a sample of the formulation utilizing a particle sizing instrument (Multisizer Model HE, Coulter Corp., Miami, FL 33116-9015) . To perform this measurement, 0.25 mL of the crystal formulation was added to 100 mL of a diluent consisting 14 mM dibasic sodium phosphate, 16 mM glycerol, 1.6 mg/mL m-cresol, 0.65 mg/mL phenol, pH 7.4. The instrument aperture tube orifice size was 50 microns. Particle size data was collected for 50 seconds. This measurement showed that the mean particle diameter of the crystals was approximately 6 microns with an approximately normal distribution encompassing a range of particle sizes from approximately 2 microns to approximately 9 microns. This result is similar to the particle size distribution of commercial NPH determined using an analogous method [DePelippis, M. R., et a.1. J. Pharmaceut. Sex. 87:170-176 (1998)3 . Preparation 15 Co-crystal suspension formulation comprising human insulin and B29-Ne-octanoyl-human insulin An acidic solution of B29-Ne-octanoyl-human insulin was prepared by dissolving 30.3 mg of B29-Ne- octanoyl-human insulin in 0.75 mL of 0.1 N HC1. An acidic solution of human insulin was prepared by dissolving 59.7 mg of human insulin (zinc crystals) in 1.5 mL of 0.1 N HC1. An aliquot (0.25 mL) of the human insulin solution was combined with the 0.75 mL B29-Ne-octanoyl-human insulin solution, giving a total volume of 1 mL, which was stirred for approximately 5 minutes. To this was added, with stirring, 0.365 mL of a 1000 ppm zinc(II) solution- To the insulin plus zinc solution was added 4 mL of crystallization diluent (40 mg/mL glycerol, 35 mM sodium phosphate, dibasic buffer, 4 mg/mL m-cresol, 1.625 mg/mL phenol, 15 mM trisodium citrate, pH 7.4) . The pH of the resulting solution was adjusted to 7.60. The solution was filtered through a 0.22 micron, low protein binding filter. Five milliliters (5 mL) of protamine solution (37.9 mg of protamine sulfate in 50 mL of water) was added to 5 mL of the filtered insulin plus zinc solution. The resulting solution was allowed to stand undisturbed for 48 hours at a controlled temperature of 25°C. Microscopic inspection (at 48 hours) revealed that crystallization had occurred and that the preparation had yielded uniform, single, rod-like crystals possessing approximate average lengths of 5 microns. To prepare for HPLC analysis and dissolution testing, the crystals were sedimented by allowing the formulation to stand undisturbed. Eight milliliters (8 mL) of the supernatant were then removed and replaced with 8 mL of a diluent [16 mg/mL glycerol, 14 mM sodium phosphate dibasic buffer, 1.6 mg/mL m-cresol, 0.65 mg/mL phenol, 6 mM trisodium citrate, pH 7.6]. The crystals were then resuspended. This procedure was carried out in the same way three times, except that on the third occasion the 8 mL of supernatant was replaced with 7 mL of diluent. The dissolution rate was determined essentially as described in Preparation 13, above. The approximate time required for 0.005 mL of the present formulation to dissolve was more than 300 minutes. The time required for a 0.005 mL sample of D100 commercial Humulin N to dissolve under the same conditions was about 10 minutes. Total potency, and potency in the supernatant, were determined by HPLC, essentially as described in Preparation 13. The total potency was 3.44 mg/mL- The concentration of soluble human insulin and B29-Ne-octanoyl- human insulin in the crystal formulation was determined to be 0.01 mg/mL. The proportions of human insulin and B29-Ne- octanoyl-human insulin in the crystal phase were determined, essentially by the procedure of Preparation 13, to be 25.5% human insulin, and 74.5% B29-Ne-octanoyl-human insulin. The mean particle diameter of the crystals, determined as described in Preparation 14, was approximately 6 microns, with an approximately normal distribution, encompassing a range of particle sizes from approximately 2 microns to approximately 12 microns. This result is similar to the particle size distribution of commercial NPH as reported in DeFelippis, M. R., et al. supra. Preparation 16 Three co-crystal formulations compared with an insulin formulation An acidic solution of B29-Ne-octanoyl-human insulin was prepared by dissolving 24.18 mg of B29-Ne- octanoyl-human insulin in 0.6 mL of 0.1 N HC1. An acidic solution of human insulin was prepared by dissolving 41.1 rag of human insulin (as zinc crystals) in 1 raL of 0.1 N HC1. Four 0.4 mL solutions were prepared by combining different volumes of the B29-Ne-octanoyl-human insulin and human insulin solutions as indicated below in Table 4. To each of the four 0.4 mL solutions, 0.15 mL of a 1000 ppm zinc(II) solution was added. To each of the four 0.55 mL solutions, 1.6 mL of a crystallization diluent (50 mM tris buffer, 10 mg/mL phenol, 100 mM trisodium citrate, with a pH of 7.6) were added. Each of the four solutions was adjusted to pH 7.6 with small quantities of 1 N NaOH and 0.1 N HC1. Each solution was filtered through a 0.22 micron, low protein binding filter. Two milliliters (2 mL) of each of the four protein solutions were combined with 2 mL of protamine solution {7.34 mg of protamine sulfate in 10 mL of water) . In each case, a precipitate formed immediately. These four 4 mL suspensions were allowed to stand undisturbed at room temperature (approximately 22°C) for 16 hours. Microscopic inspection (at 16 hours) revealed that each of the four preparations had yielded uniform, single, rod-like crystals with approximate average lengths of about 10 microns. Each 4 mL formulation was transferred to a test tube and centrifuged in a bench-top centrifuge at 3000 rpm for 20 minutes to fully sediment the crystals. For each formulation, 3 mL of the supernatant were removed and replaced with 3 mL of a diluent (25 mM tris buffer, 5 mg/mL phenol, 16 mg/mL glycerol, pH 7.4) . The crystals were then resuspended. This procedure was carried out three times except that on the third occasion the 3 mL of supernatant was replaced with 2.5 mL of diluent for each formulation. Each of the four formulations was analyzed by HPLC to quantitate the total potencies of the formulations and the compositions of the respective crystals, essentially as described above. The total potency refers to the total concentration of human insulin and B29-Ne-octanoyl-human insulin. The total potency and percentage of B29-Ne- octanoyl-human insulin were determined by analyzing an aliquot of the uniformly suspended formulation. The supernatant was analyzed to determine the total concentration of soluble human insulin and soluble B29-Ne- octanoyl-human insulin present in each formulation. The results of these analyses are presented below. Dissolution times were determined as described above in Preparation 13. Preparation 17 Preparation of insoluble compositions The following is an outline of another method that was used to prepare precipitates and micro-crystals of the present invention. The outline is to be read together with the data in Table 6, below. A measured mass of a derivatized protein, prepared as described herein, was dissolved in 0.6 mL of 0.1 N HC1. A measured mass of a protein was dissolved in 0.2 mL of 0.1 N HC1 (zinc crystals of human insulin or LysB28,Pro29-human insulin analog). The two solutions were thoroughly mixed together by stirring for five to ten minutes. A volume (0.32 mL) of an aqueous solution containing 1000 ppm Zn(II) and a volume (3.2 mL) of a diluent solution (about 50 mM Tris reagent, about 10 tag/ mL phenol, about 16 mg/mL glycerol, and about 29.5 mg/mL trisodium citrate) were added to the mixture of the two proteins. The pH of the resulting solution was adjusted to about 7.6 (7.55-7.64) using 1 N HC1 or 1 N NaOH. The pH-adjusted solution was filtered through a 0.22 micron, low-protein binding filter. To four milliliters of the filtrate was added four milliliters of a solution of protamine in water (about 37.3 mg protamine sulfate per 100 mL, range 37.18-37.48). Precipitate formed immediately upon adding the protamine solution. The preparation was allowed to stand undisturbed at 25°C. Dissolution tests were carried out as previously described. Under the same conditions, insulin NPH dissolved in about 6 minutes. The following is an outline of another method that was used to prepare precipitates and micro-crystals of the present invention. The outline is to be read together with the data in Table 7, below. A measured mass of a derivatized protein, prepared as described herein, was dissolved in 3.2 mL of diluent solution (about 50 mM Tris reagent, about 10 mg/ mL phenol, about 16 mg/mL glycerol, and about 29.5 mg/mL trisodium citrate) . A measured mass of a protein was dissolved in 0.6 mL of 0.1 N HC1 (zinc crystals of human insulin or LysB28,Pro29-human insulin analog). The two solutions were thoroughly mixed together by stirring for five to ten minutes. The pH of the resulting solution was adjusted to about 7.6 (7.55-7.64) using 1 N HCl or 1 N NaOH. The pH- adjusted solution was filtered through a 0.22 micron, low- protein binding filter. To a volume of the filtrate was added an equal volume of a solution of protamine in water (about 37.3 mg protamine sulfate per 100 mL, range 37.18- 37.48). Precipitate formed immediately upon adding the protamine solution. The preparation was allowed to stand undisturbed at 25°C. Dissolution tests were carried out as previously described. Under the same conditions, insulin NPH dissolved in about 6 minutes. The following is an outline of another method that was used to prepare precipitates and micro-crystals of the present invention. The outline is to be read together with the data in Table 8, below. A measured mass of a derivatized protein, prepared as described herein, was dissolved in a measured volume of 0.1 N HCl. A measured mass of a protein was dissolved in a measured volume of 0.1 N HCl (zinc crystals of human insulin or LysB28, Pro29-human insulin analog). Measured volumes of each of the two solutions were thoroughly mixed together by stirring for five to ten minutes. Measured volumes of an aqueous solution containing 1000 ppm Zn(II) and of a diluent solution (about 50 mM Tris reagent, about 10 mg/ mL phenol, about 32 mg/mL glycerol, and about 30 mg/mL trisodium citrate dihydrate, pH 8.47) were added to the mixture of the two proteins. The pH of the resulting solution was adjusted to about 7.6 (7.58-7.63) using 1 N HC1 or 1 N NaOH. The pH- adjusted solution was filtered through a 0.22 micron, low- protein binding filter. To two milliliters of the filtrate was added two milliliters of a solution of protamine in water (about 37.5 mg protamine sulfate per 100 mL). Precipitate formed immediately upon adding the protamine solution. The preparation was allowed to stand undisturbed at 25ºC. Dissolution tests were carried out as previously described. Under the same conditions, insulin NPH dissolved in about 6 minutes. Preparation 18 Preparation of an Amorphous Suspension A measured mass (13.84 mg of protein) of solid B28-tetradecanoyl-Lys(B28),Pro(B29) human insulin analog was dissolved in 0.375 mL of 0.1 N HC1. A measured mass of zinc human insulin (7.40 mg protein) was dissolved in 207 microliters of 0.1 N HC1. An aliquot (125 uL) of the insulin solution (containing 4.47 mg of human insulin) was added to the solution of B28-tetradecanoyl- Lys(B28),Pro(B29)-human insulin analog. A volume (180 µL) of 1000 ppm zinc and 2.0 mL of diluent (1.6 mg/mL phenol, 4 mg/mL m-cresol, 40 mg/mL glycerol, 5 mg/mL anhydrous sodium dibasic phosphate, 7.5 mg/mL trisodium phosphate dihydrate, pH 7.6) were added. The pH was increased from 5.6 to 8.0 with 100 microliters of IN NaOH and back to 7.59 with 20 microliters of IN HCl and IN NaOH. The concentration of B28-tetradecanoyl-Lys(B28),Pro(B29) human insulin analog was 4.94 mg/mL and the human insulin concentration was 1.60 mg/mL. The solution was passed through a 0.22 micron, low- protein binding filter and refrigerated overnight. The next morning, the solution had no precipitate present. To 2.50 mL of the solution was added 2.88 mL of a protamine solution (0.75 mg/mL of solid protamine sulfate dissolved in water) . An amorphous precipitate formed when the protamine was added. After adding the protamine, the concentration of B28-tetradecanoyl-Lys(B28) ,Pro(B29) human insulin analog and human insulin in the soluble phase was again determined. Samples for HPLC analysis were prepared promptly after the protamine was added. From peak retention times, HPLC analysis showed that the insoluble material in the suspension contained protamine, B28-tetradecanoyl- Lys(B28) ,Pro(B29) human insulin analog, and human insulin. The concentration of B28-tetradecanoyl-Lys(B28) ,Pro(B2S) human insulin analog in the soluble phase was 2.30 mg/mL and the concentration of human insulin was 0.74 mg/mL. The concentrations of B28-tetradecanoyl- Lys (B28) ,Pro(B29) human insulin analog and human insulin in acidified samples of the suspension, supernatant, and precipitate were determined and are tabulated below. They are in reasonable agreement with expected values. Protamine concentrations were not quantitated. The following is an outline of another method used for preparing precipitates of the present invention. The method was used to prepare formulations of amorphous precipitates of insulin with each of three derivatized proteins: B29-Ne-octanoyl-huraan insulin; B29-Ne-nonanoyl- human insul in; and B2 8 -Ne- octanoyl - LysB2 8, ProB2 9 - human insulin analog. A measured mass of solid derivatized protein was dissolved in 3 mL of 0.1 N HC1 to produce a solution containing approximately 16 mg/mL derivatized protein. A measured mass of zinc human insulin crystals (73 rag, of which 67.17 mg was protein) was dissolved in 4.198 mL of 0.1 N HC1 to produce a solution containing approximately 16 mg/mL insulin). Three milliliters of the solution of derivatized protein and one milliliter of the insulin solution were combined and thoroughly mixed. Measured volumes of a 1000 ppm zinc solution (1.137 mL) and of a diluent (16 mL, containing, per mL: 1.625 mg phenol, 4 rag m- cresol, 40 mg glycerol, 5 mg anhydrous sodium dibasic phosphate, 7.5 mg trisodium citrate dihydrate, pH 7.6) were added. The pH was adjusted to about 7.6 (7.58-7.61) using 5 N NaOH and 5 N HC1 solutions. The volume added during pR adjustment was from 0.11 to 0.12 mL. The solution was passed through a 0.22 micron, low-protein binding filter and refrigerated overnight. The next morning, the solution had no precipitate present. The solution was comprised of protein and derivatized protein (approximately a 1:3 mass ratio), and the total protein concentration was equivalent to about 85 units per milliliter. Just prior to testing in rats, equal volumes of the solution and of a solution of protamine sulfate (0.352 mg/mL) were combined and mixed thoroughly. An amorphous precipitate formed immediately. A sample of the suspension formulation containing the amorphous precipitate was promptly injected into test animals. After mixing with protamine, the concentration of total protein was about 42.4 units/ml. Preparation 20 Gly(A21), Arg(B31), Arg(B32)-Human Insulin Analog Gly(A21)Arg(B31)Arg(B32)-human insulin was obtained from an E. coli fermentation in which a Gly(A21)- human proinsulin precursor molecule was overexpressed into inclusion bodies. A portion (94.7 g) of inclusion bodies was solubilized in 500 mL of 6 M guanidine hydrochloride containing 0.1 M TRIS, 0.27 M sodium sulfite, and 0.1 M sodium tetrathionate, pH 10.5 at room temperature. The pH was quickly lowered to 8.8 with 12 N HC1. After vigorously stirring in an open container for 45 minutes the pH was lowered to 2.1 with phosphoric acid and the sample centrifuged overnight at 4°C. The supernatant was decanted and stored at 4°C for additional processing. The pellet was re-extracted with 200 mL of additional pH 10.5 solution (see above) and then centrifuged for 3 hours at 4°C. This and the previously obtained supernatant were each diluted 4X with 100 mM sodium phosphate, pH 4, precipitating the product and other acidic components. After allowing the precipitate to settle, most of the supernatant was decanted and discarded. The resulting suspension was centrifuged, followed by decanting and discarding of additional supernatant, leaving wet pellets of the crude Gly(A2X)-human proinsulin S-sulfonate precursor. The pellets were solubilized in 1.5 liters of 7 M deionized urea, adjusting the pH to 8 with 5 N NaOH and stirring over several hours at 4°C. Salt (NaCl) was then added to achieve l M concentration and the sample was loaded onto a XAD-7 column (14 cm X 20 cm, Toso-Haas, Montgomeryville, PA) , previously flushed with 50% acetonitrile/50% 50 mM ammonium bicarbonate, 10% acetonitrile/90% 50 mM ammonium bicarbonate, and finally with 7 M deionized urea/lM NaCl/20 mM TRIS, pH 8. Once loaded, the column was pumped with 4.5 liters of a 7 M deionized urea/1 M NaCl/20 mM TRIS, pH 8 solution, followed by 2.8 liters of 50 mM ammonium bicarbonate/1 M NaCl, and 6.5 liters of 50 mM ammonium bicarbonate. The column was eluted with a linear gradient of acetonitrile in 50 mM ammonium bicarbonate, while monitoring the eluant by UV at 280 nm. The peak of interest, partially purified Gly(A21)-human proinsulin S- sulfonate precursor, was collected, lyophilized, and subjected to a folding/disulfide bond procedure as follows. A quantity (5.4 g) of the precursor was dissolved in 3 liters of 20 mM glycine, pH 10.5, 4°C. Then, 15 mL of 240 mM cysteine HC1 were added with stirring, while maintaining the pH at 10.5 and the temperature at 4°C. The reaction solution was stirred gently at 4°C for 27 hours and then quenched by lowering the pH to 3.1 with phosphoric acid. Acetonitrile (155 mL) was added, and the solution was then loaded onto a 5 x 25 cm C4 reversed-phase column previously pumped with 60% acetonitrile/40% water/0.1% TFA and equilibrated in 10% acetonitrile/90% water/0.1% TEA. Once loaded the column was pumped with 1 liter of 17.5% acetonitrile/82.5% water/0.1% TFA, then eluted with a linear gradient of acetonitrile in 0.1% TFA while monitoring at 280 nm. Selected fractions were pooled and lyophilized with a recovery of 714 mg. For conversion of the proinsulin precursor to the desired insulin analog, 697 mg of the Gly(A21) human proinsulin precursor were dissolved in 70 mL 50 mM ammonium bicarbonate, then chilled to 4°C, pH 8.3. A volume (0.14 mL) of a 1 mg/mL solution of pork trypsin (Sigma Chemical Company, St. Louis, Mo) in 0.01 N HC1 was added to the sample solution which was stirred gently at 4°C for about 24 hours. An additional 0.14 mL of the trypsin solution was added to the reaction solution which was then stirred for an additional 21 hours, 45 minutes. The reaction was quenched by lowering the pH to 3.2 with 0.7 mL glacial acetic acid and 0.3 mL phosphoric acid. The quenched Gly(A21)Arg(B31)Arg(B32)-human insulin sample solution from the tryptic cleavage reaction was diluted 4X with 30% acetonitrile/70% 50 mM acetic acid, pH 3.1, and loaded onto a 1 x 30 cm S HyperD F (Biosepra, Marlborough, MA) cation exchange column previously pumped with 30% acetonitrile/70% 50 mM acetic acid/500 mM NaCl, pH 3.3, and equilibrated in 30% acetonitrile/70% 50 mM acetic acid. Once loaded the column was pumped with about 50 mL of 30% acetonitrile/70% 50 mM acetic acid, then eluted with a linear gradient of NaCl in 30% acetonitrile/50 mM acetic acid while monitoring the eluant at 276 nm. Selected fractions containing the Gly(A21)Arg(B31)Arg(B32)-human insulin were pooled, diluted 3X with purified water and loaded onto a 2.2 x 25 cm C4 reversed-phase column (Vydac, Hesperia, CA) previously pumped with 60% acetonitrile/40% water/0.1% TFA, then 10% acetonitrile/90% water/0.1% TFA. Once loaded, the column was pumped with about 200 mL of 10% acetonitrile/90% water/0.1% TFA, then eluted with a linear gradient of acetonitrile in 0.1% TFA. Selected fractions were pooled and lyophilized giving a recovery of 101 rag. Analytical HPLC revealed a purity of greater that 95% main peak. Electrospray mass spectroscopy (ESMS) analysis of the purified protein yielded a molecular weight of 6062.9 (6063.0, theory). Preparation 21 Des(B30)-husan insulin Des(B30)-human insulin was prepared from human proinsulin by controlled tryptic hydrolysis. A mass (2 g) of human proinsulin biosynthesized in recombinant E. coli and purified by conventional methods [Frank, B. h. , et al., in PEPTIDES: Synthesis-Structure-Function. Proceedings of the Seventh American Peptide Symposium, Rich, D. H. and Gross, E. (Eds.), Pierce Chemical Company, Rockford, pp. 729-738, 1981; also, Frank, B. H., U. S. Patent No. 4,430,266, issued 7 February 1984, each of which is incorporated by reference] were dissolved in 400 mL of o.l M, pH 7.5 HEPES buffer. After addition of 8 mL of 1 M CaCl2 (in water) and pH adjustment to 7.5 with 5 N NaOH, 2 mL of a 10 mg/mL solution of pork trypsin (Sigma) in 0.01 N HC1 were transferred to the sample solution while gently stirring. The reaction solution was allowed to stir at ambient temperature for 2 hours and 42 minutes, at which time it was transferred to a 37°C environment while stirring occasionally. After 1 hour and 45 minutes at 37°C the enzymatic reaction was quenched by lowering the pH to 3.0 with phosphoric acid and the temperature to 4°C for storage. Subsequently, the solution was brought to room temperature and diluted with 50 mL acetonitrile, then to a final volume of 500 mL with purified water, then loaded onto a 2.5 x 58 cm CG-161 (Toso-Haas) column previously pumped with 1 c.v. (column volume) of 40% acetonitrile/60% 0.1 M ammonium sulfate, pH 2.5, and 2 c.v. of 10% acetonitrile/90% 0.1 M ammonium sulfate, pH 2.5. Once loaded, the column was pumped with 1 c.v. of 10% acetonitrile/90% 0.1 M ammonium sulfate, pH 2.5. The column was eluted with a linear gradient of acetonitrile in 0.1 M ammonium sulfate, pH 2.5, while monitoring the eluant at 276 nm. The peak of Interest, partially purified des(B30)-human insulin, was collected by pooling selected fractions. This pooled sample of partially purified des(B30)-human insulin was diluted to 1.28 liters with purified water, pH 3.5, and applied to a 1 x 29 cm S HyperD F (Biosepra) cation exchange column previously pumped with 1 c.v. of 30% acetonitrile/70% 0.1% TFA/0.5 M NaCl, pH 1.9, and 2 c.v. of 30% acetonitrile/70% 0.1% TEA, pH 2.3. Once loaded the column was pumped with 1 c.v. 30% acetonitrile/70% 0.1% TFA, pH 2.3, then eluted with a linear gradient of NaCl in 30% acetonitrile/70% 0.1% TFA, pH 1.9 to 2.3, while monitoring the eluant at 276 nm. Selected fractions containing the purified des(B3 0)-human insulin were pooled, diluted 2.5X with purified water and loaded onto a 35-c.c. C8 SepPak (Waters, Milford, MA) previously cleaned and primed with 2 c.v. of acetonitrile, 2 c.v. of 60% acetonitrile/40% 0.1% TFA, and 2 c.v. of 10% acetonitrile/90% 0.1% TFA. Once loaded the SepPak was flushed with 3 c.v. of 10% acetonitrile/90% 0.1% TFA and then eluted with 2 c.v. of 60% acetonitrile/40% 0.1% TFA. The lyophilized eluant yielded 500 mg. An analytical HPLC assay suggested greater than 95% main peak. Electrospray mass spectroscopy (ESMS) analysis of the purified protein yielded a molecular weight of 5706.5 (5707, theory). Preparation 22 Rabbit Insulin Rabbit insulin was prepared as described in Chance, R. E., et al. [Proinsulin, Insulin, C-Peptide, Baba, S., et al. (Eds.), Excerpta Medica, Amsterdam-Oxford, pp. 99-105 (1979)]. Preparation 23 Asp(B28)-Human Insulin Analog Asp(B28)-human insulin was prepared and purified essentially according to the teaching of examples 31 and 32 of Chance, R. E., et al- (U. S. Patent No. 5,700,662, issued 23 December 1997) which is expressly incorporated herein by reference. Des(B23-30)-human insulin iBromer, W. W. and Chance, R. E., Biochim. Biophys. Acta, 133:219-223 (1967), which is incorporated herein by reference] and a synthetic octapeptide Gly-Phe-Phe-Tyr-Thr-Asp-Lys (Tfa) -Thr were condensed using trypsin-assisted semisynthesis, purified by gel filtration and reversed-phased HPLC, treated with 15% ammonium hydroxide (v/v) for four hours at ambient temperature to remove the trifluoroacetate (Tfa) blocking group from Lys(B29), purified by reversed-phase HPLC, and lyophilized. Preparation 24 Syntheses of derivatized proteins The following is an outline of the syntheses of certain derivatized proteins used to prepare the precipitates and microcrystals of the present invention. The outline is to be read together with the data in Table 10, below. A measured mass of purified insulin or of an insulin analog was dissolved in a measured volume of dimethylsulfoxide (DMSO) with stirring. Then, a measured volume of tetramethylguanidine hydrochloride (TMG) was added and the solution mixed thoroughly. In a separate container, a measured mass of an N-acyl-succinimide (NAS) was dissolved in a measured volume of DMSO. A measured volume of the second solution was added to the first solution. The reaction was carried out at room temperature, and the progress of the reaction was monitored by analyzing samples of the reaction mixture using HPLC. The reaction was quenched by adding a measured volume of ethanolamine, and then acidifying to pH 2-3. The reaction mixture was then subjected to purification using reversed-phase chromatography alone, or using a combination of cation exchange chromatography followed by reversed-phase chromatography. The reversed- phase purification was carried out using an FPLC system (Pharmacia) with UV detection at 214 nm or at 280 nm, a fraction collector, 2.2 x 25 cm or 5 x 30 cm C18 column, 2.5 or 5 mli/min flow rate, at room temperature. The liquid phases were mixtures of Solution A [0.1% trifluroacetic acid (TFA) in 10:90 acetonitrile:water (vol:vol)] and Solution B [0.1% trifluroacetic acid (TFA) in 70:30 acetonitrile:water (vol:vol)] appropriate to elute and separate the species of interest. Typically, the- column was equilibrated and loaded while in 100% Solution A. Then, a linear gradient to some proportion of Solution B was used to separate the reaction products adequately. Fractions containing product were pooled. The development of purification methods is within the skill of the art. Table 10 below provides experimental data, according to the outline above, for the synthesis of the derivatized proteins that were used to prepare various embodiments of the present invention. The starting proteins were prepared as described above, or according to conventional methods. Conventional purification was used to provide highly purified starting proteins for the syntheses described below. The synthesis of insulin, insulin analogs, and proinsulin is within the skill of the art, and may be accomplished using recombinant expression, semisythesis, or solid phase synthesis followed by chain combination. The purification of synthesized proteins to a purity adequate to prepare the derivatives used in the present invention is carried out by conventional purification techniques. Molecular weight of the purified derivatives was confirmed by mass spectrometry via electrospray mass analysis (ESMS) . Assignment of the acylation site was based either on a chromatographic analysis ('HPLC), or on an N- terminal analysis ("N-terminal"), or both. The following xs an outline of the synthesis of additional derivatized proteins. The outline is to be read together with the data in Table 11, below, to provide full synthetic schemes. A measured mass of purified insulin or of an insulin analog was dissolved by adding to it a measured volume of 50 mM boric acid, pH 2.57. A measured volume of acetonitrile, equal to the volume of boric acid solution, was then added slowly with stirring. The "solvent' volume is the sum of the volumes of the boric acid and acetonitrile. The pH of the solution was adjusted to between 10.2 and 10.5 using NaOH. In a separate container, a measured mass of an N-acyl-succinimide ("NAS") was dissolved in a measured volume of DMSO. A measured volume of the second solution was added to the first solution. The reaction was carried out at room temperature, the pH was maintained above 10.2 as necessary, and the progress of the reaction was monitored by analyzing samples of the reaction mixture using HPLC. The reaction was quenched by acidifying to pH 2-3. The reaction mixture was then subjected to purification using a reversed-phase chromatography system as described above. Table 11 provides experimental data, according to the outline above, for the synthesis of the derivatized proteins that were used to prepare various embodiments of the present invention. Molecular weight of the purified derivatives was confirmed by mass spectrometry via electrospray mass analysis (ESMS). Assignment of the acylation site was based either on a chromatographic analysis ("HPLC"), or on an N-terminal analysis ("N- terminal"), or both. The following is a general outline of a synthetic scheme to produce additional derivatized proteins. In a specific instance, the outline is to be read together with the data in Table 12, below, to a provide full synthetic scheme for a particular derivatized protein. A measured mass of purified insulin or insulin analog was dissolved by adding to it a measured volume DMSO. The pH of the solution was adjusted with 10 equivalents of tetramethylguanidine. In a separate container, a measured mass of an N-acyl- succinimide CNAS") was dissolved in a measured volume of DMSO. A measured volume of the second solution was added to the first solution to provide a 1.9 fold molar excess of N- acyl-succinimide. The reaction was carried out at room temperature and the progress of the reaction was monitored by analyzing samples of the reaction mixture using HPLC. The reaction was quenched with 20 microliters of ethanolamine, chilled in ice/water bath and diluted 2.1 times with 0.IN HC1. The reaction mixture was then subjected to desalting on reversed phase chromatography column using the following protocol: l) the column was wetted with 100% acetonitrile, then was washed using three to four column volumes of 0.1% TFA/70% acetonitrile (Buffer B); and finally was washed using four to five column volumes of 0.1% TFA/10% acetonitrile (Buffer A); 2) diluted reaction mixtures were loaded, and the column was again washed with five to six column volumes of Buffer A; and 3) the derivatized protein was eluted by passing five to six column volumes of Buffer B through the column. The fluid collected during elution was frozen, then lyophilized. The lyophilized crude product (86.1 mg) was then subjected to re-purification using a reversed-phase chromatography system as described above. Table 12 provides experimental data, according to the outline above, for the synthesis of the derivatized proteins that were used to prepare various embodiments of the present invention. Molecular weight of the purified derivatives was confirmed by mass spectrometry via electrospray mass analysis (ESMS). Assignment of the acylation site was based either on a chromatographic analysis ("HPLC") . Experiment 1 Time Action of Co-crystals in Dogs The time-action of three co-crystal compositions of the present invention was determined in normal dogs that received a constant infusion of somatostatin to create a transient diabetic state. The first co-crystal formulation, comprising human insulin and B29-Ne-octanoyl-human insulin, was prepared essentially as described for Formulation D in Preparation 16 above, and was administered subcutaneously at a dose of 3 nmol/kg ("8753"). The second co-crystal formulation, comprising human insulin and B29-Ne-octanoyl- human insulin, was prepared as described for Formulation D in Preparation 16 above, and was administered subcutaneously at a dose of 2.5 nmol/kg (-8752.5") . Finally, a third co- crystal formulation, comprising human insulin and B29-Ne- decanoyl-human insulin, was prepared as described in Preparation 14 above, and was administered subcutaneously at a dose of 2.5 nmol/kg ("10252.5") . The data were compared to that observed in the same model after administration of Humulin N (2.0 nmol/kg "NPH"), Beef/Pork Ultratlente insulin (3 nmol/kg, "BP-UL"), and saline. Experiments were conducted in overnight-fasted, chronically cannulated, conscious male and female beagles weighing 10-17 kg (Marshall Farms, North Rose, NY) . At least ten days prior to the study, animals were anesthetized with isoflurane (Anaquest, Madison, WI), and silicone catheters attached to vascular access ports (V-A-P™, Access Technologies, Norfolk Medical, Skokie, ID were inserted into the femoral artery and femoral vein. The catheters were filled with a glycerol/heparin solution (3:1, v/v; final heparin concentration of 250 KlU/ml; glycerol from Sigma Chemical Co., St. Louis, MO, and heparin from Elkins- Sinn, Inc., Cherry Hill, NJ) to prevent catheter occlusion, and the wounds were closed. Kefzol (Eli Lilly & Co., Indianapolis, IN) was administered pre-operatively (20 mg/kg, IV and 20 mg/kg, I.M.), and Keflex was administered post-operatively (250 mg, p.o. once daily for seven days) to prevent infections. Torbugesic (1.5 mg/kg, I.M.) was administered post-operatively to control pain. Blood was drawn just prior to the study day to determine the health of the animal. Only animals with hematocrits above 38% and leukocyte counts below 16,000/mm3 were used (hematology analyzer: Cell-Dyn 900, Sequoia- Turner, Mountain View, CA). The morning of the experiment, the ports were accessed (Access Technologies, Norfolk Medical, Skokie, IL) ,- the contents of the catheters were aspirated; the catheters were flushed with saline (Baxter Healthcare Corp., Deerfield, IL); the dog was placed in a cage; and extension lines (protected by a stainless steel tether and attached to a swivel system [Instech Laboratories, Plymouth Meeting, PA]) were attached to the port access lines. Dogs were allowed at least 10 minutes to acclimate to the cage environment before an arterial blood sample was drawn for determination of fasting insulin, glucose, and glucagon concentrations (time - -30 minutes). At this time, a continuous, IV infusion of cyclic somatostatin (0.65 µg/kg/min; BACHEM California, Torrance, CA) was initiated and continued for the next 30.5 hours. Thirty minutes after the start of infusion (time = 0 minutes) , an arterial blood sample was drawn, and a subcutaneous bolus of test substance, or vehicle, was injected in the dorsal aspect of the neck. Arterial blood samples were taken every 3 hours thereafter for the determination of plasma glucose and insulin concentrations and every 6 hours for determination of plasma glucagon concentrations. The entire study lasted 3 0 hours. Arterial blood samples were collected in vacuum blood collection tubes containing disodium EDTA (Terumo Medical Corp., Elkton, MD) and immediately placed on ice. A portion of the blood sample (1.5 ml) was transferred to a polypropylene tube containing 40 ul of aprotinin (10,000 KID/ml; Trasylol, Miles, Inc., Diagnostics Division, Kankakee, IL) in preparation for the determination of the plasma glucagon concentration. The samples were centrifuged, and the resulting plasma was transferred to polypropylene test tubes and stored on ice for the duration of the study. Plasma glucose concentrations were determined the day of the study using a glucose oxidase with a commercial glucose analyzer. Samples for other assays were stored at - 80° C until time for analysis. Insulin concentrations were determined using a double antibody radioimmunoassay. Glucagon concentrations were determined using a radioimmunoassay kit (LINCO Research, Inc., St. Charles, MO) . At the conclusion of the experiment, the catheters were flushed with fresh saline, treated with Kefzol (20 rag/kg), and filled with the glycerol /heparin mixture; antibiotic (Keflex; 250 mg) was administered p.o. To minimize the number of animals being used ami to allow pairing of the data base when possible, animals were studied multiple times. Experiments in animals being restudied were carried out a minimum of one week apart. The 1:3 co-crystal of human insulin and B29-Ne- octanoyl-human insulin had a time-action 9 hours longer than NPH human insulin (24 hours vs. 15 hours) for the higher dose (8753) , and a time-action 6 hours longer than NPH human insulin (21 hours vs. 15 hours) for the lower dose (8752.5). The time-action was determined by statistically comparing the mean glucose levels with those of the control group (saline). The glucose profiles for the 1:3 co-crystal formulations of human insulin and B29-Ne-octanoyl-human insulin were more like that expected of a basal insulin than was the profile for NPH-human insulin. The 1:3 co-crystals also had greater activity and a more desirable glucose profile than did Beef/Pork Ultralente insulin. The reduction in blood glucose, compared with the control (saline), that the co-crystal formulations caused persisted longer than that caused by this Beef/Pork Ultralente insulin. The 3:1 co-crystal formulation of human insulin and B29-Ne-decanoyl-human insulin (10252.5) had a time- action 9 hours longer than NPH human insulin (24 hours vs. 15 hours) . The difference was significant statistically (p<0.05). In the same animals, the 3:1 co-crystal formulation of human insulin and B29-N6-decanoyl-human insulin (2.5 nmol/kg, SO had a time-action 6 hours longer than either Humulin U or Beef U preparations (24 hours vs. 18 hours) . The differences were also significant statistically (p<0.05). The glucose profile for the co- crystal formulations was more like that expected of a basal insulin than was the profile for NPH-human insulin. Furthermore, the variability in time-action among the dogs was the least when the 3:1 co-crystal was administered. In conclusion, these data demonstrate that the co- crystals of the present invention are effective fox controlling glucose levels for protracted periods of time in dogs. They also support a conclusion that the co-crystals of the present invention will be effective for overnight glucose control of patients with type 2 diabetes or as the basal arm of basal/bolus insulin therapy for patients with type 1 or type 2 diabetes. They also suggest that these preparations may produce less variable responses than commercially available insulin preparations. Experiment 2 Time Action of Co-crystals in Pigs Studies were performed on normal, conscious female pigs weighing 17-25 kg. An arterial (carotid or femoral) catheter was surgically pre-implanted for sampling along with jugular venous lines for the administration of somatostatin. Prior to experiments, the cannulated pigs were fasted 22-24 hours. Subcutaneous insulin injections were given in the soft skin behind the ear at a dosage of 3.0 nmol/kg (0.5 unit/kg). Somatostatin was administered concurrently at 0.3 µg/kg/min (dissolved in 0.9% NaCl containing 1% human serum albumin, Miles Canada, Etobicoke, ON) to suppress endogenous insulin secretion. Near normoglycemia was maintained by infusing 20% dextrose at a variable rate, with frequent monitoring of glucose concentrations. The plasma glucose levels were determined on fresh plasma samples the day of the study using a glucose oxidase method with a commercial glucose analyzer. In a euglycemic clamp study, a formulation of the present microcrystals comprised of 1:3 insulin:B29-Ne- octanoyl-human insulin was administered subcutaneously at a dose of 0.5 U/kg (equivalent to about 3 nmol/kg) at the start of the study (time 0) to five pigs. The rate of glucose infusion required to maintain euglycemia (set point = about 90 mg/dL) was determined continuously. A control group received Humulin N (U100) by subcutaneous administration at the same dose (n=6) . A concomitant infusion of somatostatin (0.3 µg/kg/min) was maintained for the entire duration of the experiment. For the microcrystals of the present invention, the glucose infusion rate increased steadily over the first two hours, reaching a maximum of about 7 mg/kg/min. From then, until about 17.5 hours, the glucose infusion rate decreased fairly steadily to about 0.5 rag/kg/min. For most of the time between 17.5 hours and the end of the study at 24 hours, the glucose infusion rate remained between about 0.5 and about 2 mg/kg/min. By contrast, the mean glucose infusion rate in the control group (Humulin NPH) increased steadily, reaching a maximum of about 14 mg/kg/min at about 3 hours after administration. Thereafter, the infusion rate decreased to about 7 mg/kg/min by about 4.5 hours, and to about 5 mg/kg/min by 13 hours after administration. No further data were taken for the control group. These results are consistent with a conclusion that the microcrystalline formulation comprised of insulin and B29-Ne-octanoyl-human insulin in a 1:3 molar ratio has a flatter glucodynamic profile than does insulin NPH. Experiment 3 Tine Action of Co-crystals in Rats A formulation of the present microcrystals comprised of 1:3 insulin:B29-Ne-octanoyl-huraan insulin was tested in BBDP/Wor rats, a genetically-characterized animal model, maintained by, and available from, the University of Massachusetts Medical Center (Worchester, MA) in connection with Biomedical Research Models, Inc. (Rutland, MA). The DPBB/Wor rat line is diabetes-prone, and exhibits insulin- dependent (autoimmune) diabetes mellitus. All preparations were administered subcutaneously at a dose of 0.9 U/100 g body weight. Male BBDP/Wor rats, aged 4-5 months and maintained on a long-acting insulin (P2I), were randomly assigned to five experimental groups. A, B, C, D and E. Group A (n«22) was treated for three days with a U40 human insulin ultralente (Humulin DL); group B (n«18) was treated for 3 days with a D40 preparation of Iletin Ultralente (65% beef insulin, 35% pork insulin); group C (n-10) was treated for three days with a formulation of microcrystals comprised of 1:3 insulin:B29-Ne-octanoyl-human insulin, prepared as described above; group D (n-21) was treated with a formulation of microcrystals comprised of 100% B29-N6- octanoyl-human insulin; and group E received U40 beef-pork PZI insulin (PZI) . Each rat was given daily injections of its group's formulation for the two days before blood glucose was determined, and on the day that the blood glucose was determined. Blood was obtained half an hour before administering the test formulations. Samples of the formulations were injected at 11:30 A.M. Blood was obtained by nicking the tail (not anaesthetized) . The samples were stored briefly on ice, then were centrifuged, and glucose determined using a Beckman II glucose analyzer. Blood samples were obtained just prior to administering the test formulations, and at 2, 4, 6, 8, 12, 16, 20, and 24 hours after administration. Considering adequate control to be indicated by blood glucose levels less than 200 mg/dL, the preparations provided about 9.5 hours (Humulin DL), about 12 hours (Iletin D) , about 15.5 hours (the present invention), about 20.5 hours (100% B29-Ne-octanoyl-human insulin), and about 21.5 hours (PZI) of control. Therefore, the microcrystal formulation of the present invention controlled blood glucose longer than both Humulin DL and Iletin D and for a shorter period of time than did either the 100% B29- Ne-octanoyl-human insulin microcrystal preparation or the PZI preparation. Experiment 4 Time Actions of Amorphous Precipitates in Rats Formulations of amorphous precipitates comprised of 1:3 insulin :B2 9-Ne-octanoyl-human insulin, 1:3 insulin:B28-Ne-octanoyl-Lys (B28), Pro (B29) -human insulin, and 1:3 insulin:B29-Ne-nonanoyl-human insulin, prepared as described in Preparation 19, were tested in BBDP/Wor rats. All preparations were administered subcutaneously at a dose of 0.9 U/1O0 g body weight. Male BBDP/Wor rats, aged 4-5 months and maintained on a long-acting insulin (PZI) , were randomly assigned to five experimental groups, A, B, C, D, and E. Group A (n«7) was treated with a preparation of U40 NPH (Humulin N) . Group B (n«=8) was treated with a D42.4 preparation of 1:3 insulin:B29-Ne-octanoyl-human insulin. Group C (n=8) was treated with a U42.6 preparation of 1:3 insulin:B28-Ne- octanoyl-Lys(B28),Pro(B29)-human insulin. Group D(n=8) was treated with a D42.7 preparation of 1:3 insulin:B29-Ne- nonanoyl-human insulin. Group E was treated with D40 beef- pork PZI insulin (PZI). Blood was obtained half an hour before administering the test formulations. Animals were injected subcutaneously (0.9 D/100 g body weight) at 11:30 A.M. Blood was obtained by nicking the tail (not anaesthetized). The samples were stored briefly on ice, then centrifuged, and glucose was determined using a commercial glucose analyzer. Blood samples were obtained just prior to administering the test formulations, and at 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, and 24 hours after administration. Considering adequate control to be indicated by blood glucose levels less than 200 mg/dL, the preparations provided about 7.5 hours (1:3 insulin :B28-Ne-octanoyl- Lys(B28), Pro(B29)-human insulin), about 9 hours (NPH), about 15.5 hours (1:3 insulin:B29-Ne-octanoyl-human insulin), about 16 hours (1:3 insulin:B29-Ne-nonanoyl-human insulin) and about 22.5 hours (PZI) of control. The principles, preferred embodiments and modes of operation of the present invention have been described in the foregoing specification. The invention which is intended to be protected herein, however, is not to be construed as limited to the particular forms disclosed, since they are to be regarded as illustrative rather than restrictive. Variations and changes may be made by those skilled in the art without departing from the spirit of the invention. I claim: 1. An insoluble composition, comprising: a) a protein selected from the group consisting of insulin, insulin analog, and proinsulin; b) a derivatized protein selected from the group consisting of derivatized insulin, derivatized insulin analog, and derivatized proinsulin; c) a complexing compound; d) a hexamer-stabilizing compound; and e) a divalent metal cation. 2. The composition of Claim 1 which is an amorphous precipitate. 3. The composition of Claim 1 which is a microcrystal. 4. The composition of Claim 3, wherein the microcrystal has rod-like morphology. 5. The composition of Claim 3, wherein the microcrystal has irregular morphology. 6. The composition of Claim 1, wherein the derivatized protein is selected from the group consisting of fatty acid-acylated insulin, fatty acid-acylated insulin analogs, and fatty acid acylated proinsulins. 7. The composition of Claim 6, wherein the complexing compound is protamine, the hexamer-stabilizing compound is a phenolic preservative, and the divalent metal cation is zinc. 8. The composition of Claim 1, wherein the derivatized protein is selected from the group consisting of fatty acid-acylated insulin and fatty acid-acylated insulin analogs. 9. The composition of Claim 8, wherein the complexing compound is protamine, the hexamer-stabilizing compound is a phenolic preservative, and the divalent metal cation is zinc. 10. The composition of Claim 1, wherein the derivatized protein selected from the group consisting of acylated insulin, acylated insulin analogs, and acylated proinsulins. 11. The composition of Claim 1, wherein the derivatized protein is selected from the group consisting of acylated insulin and acylated insulin analogs. 12. The composition of Claim 11, wherein the derivatized protein is mono-acylated at its Lys-Ne-amino group. 13. The composition of Claim 12, wherein the complexing compound is protamine, which is present at about 0.15 mg to about 0.5 mg per 3.5 rag of total protein. 14. The composition of Claim 13, wherein the divalent metal cation is zinc, which is present at about 0.3 mole to about 0.7 mole per mole of total protein. 15. The composition of Claim 14, wherein the hexamer-stabilizing compound is a phenolic preservative selected from the group consisting of phenol, m-cresol, o- cresol, p-cresol, chlorocresol, methylparaben, and mixtures thereof, and is present at a ratio of at least 3 moles of phenolic preservative to 6 moles of total protein. 16. The composition of Claim 15, wherein the protein is selected from the group consisting of insulin and insulin analogs. 17. The composition of Claim 16, wherein the protein is insulin. 18. The composition of Claim 17, wherein the derivatized protein is insulin that is mono-acylated at the LysB29-Ne-amino groups 19. The composition of Claim 18, wherein the derivatized protein is insulin that is acylated with a straight-chain, saturated fatty acid. 20. The composition of Claim 19, wherein the straight-chain, saturated fatty acid is selected from the group consisting of n-hexanoic acid, n-heptanoic acid, n- octanoic acid, n-nonanoic acid, and n-decanoic acid. 21. The composition of Claim 20, wherein the mole ratio between the protein and the derivatized protein is from about 1:9 to about 9:1. 22. The composition of Claim 21, wherein the straight-chain, saturated fatty acid is selected from the group consisting of n-hexanoic acid, n-octanoic acid, and n- decanoic acid. 23. The composition of Claim 22, wherein the straight-chain, saturated fatty acid is selected from the group consisting of n-octanoic acid and n-decanoic acid 24. The composition of Claim 23, wherein the straight-chain, saturated fatty acid is n-octanoic acid. 25. The composition of Claim 24, wherein the mole ratio between the protein and the derivatized protein is from about 1:3 to about 3:1. 26. The composition of Claim 22, wherein the mole ratio between the protein and the derivatized protein is from about 1:9 to about 1:1. 27. The composition of Claim 16, wherein the protein is an insulin analog. 28. The composition of Claim 27, wherein the protein is LysB28,ProB29-human insulin analog. 29. The composition of Claim 21, wherein the protein is AspB28-human insulin analog. 30. The composition of Claim 1, wherein the protein is insulin or an insulin analog, and the derivatized protein is an acylated protein selected from the group consisting of acylated insulin and acylated insulin analogs. 31. The composition of Claim 1, wherein the derivatized protein is insulin that is mono-acylated at its LysB29-Ne amino group with a straight-chain, saturated fatty acid. 32. The composition of Claim 31, wherein the straight-chain, saturated fatty acid is selected from the group consisting of n-hexanoic acid, n-heptanoic acid, n- octanoic acid, n-nonanoic acid, and n-decanoic acid. 33. The composition of Claim 32, wherein the derivatized protein is selected from the group consisting of B29-Ne-hexanoyl-human insulin, B29-Ne-octanoyl-human insulin, and B29-Ne-decanoyl-human insulin. 34. The composition of Claim 31, wherein the straight-chain, saturated fatty acid selected from the group consisting of n-dodecanoic acid, n-tetradecanoic acid, and n-hexadecanoic acid. 35. The composition of Claim 1, wherein the derivatized protein is di-acylated at the Lys-Ne-amino group and is also acylated at one N-terminal Na-amino group, and wherein the fatty acid is selected from the group consisting of n-hexanoic acid, n-heptanoic acid, n-octanoic acid, n- nonanoic acid, and n-decanoic acid. 36. The composition of Claim 1, wherein the derivatized protein is acylated with a branched-chain, saturated fatty acid. 37. The composition of Claim 36, wherein the derivatized protein is acylated with a branched-chain, saturated fatty acid having from three to ten carbon atoms in its longest branch. 38. The composition of Claim 1, wherein the derivatized protein is an insulin analog that is mono- acylated at its Lys-Ne-amino group with a straight-chain, saturated fatty acid. 39. The composition of Claim 38, wherein the fatty acid is selected from the group consisting of n- hexanoic acid, n-heptanoic acid, n-octanoic acid, n-nonanoic acid, and n-decanoic acid. 40. The composition of Claim 38, wherein the derivatized protein is an insulin analog that is mono- acylated at the Ne-amino group with a fatty acid selected from the group consisting of n-dodecanoic acid, n- tetradecanoic acid, and n-hexadecanoic acid. 41. The composition of Claim 38, wherein the derivatized protein is selected from the group consisting of fatty acid-acylated animal insulins, fatty acid-acylated monomeric insulin analogs, fatty acid-acylated deletion analogs, and fatty acid-acylated pi-shifted insulin analogs. 42. The composition of Claim 41, wherein the derivatized protein is fatty acid-acylated des(B30)-human insulin analog, fatty acid-acylated LysB28,ProB29-human insulin analog, or fatty acid-acylated AspB28-human insulin analog. 43. The composition of Claim 42, wherein the derivatized protein is fatty acid-acylated des(B30)-human insulin analog. 44. The composition of Claim 43, wherein the derivatized protein is B29-Ne-myristoyl-des(B30)-human insulin analog. 45. The composition of Claim 42, wherein the derivatized protein is fatty acid-acylated LysB28,ProB29- human insulin analog. 46. The composition of Claim 45, wherein the derivatized protein is B28-Ne-myristoyl-LysB28,PxoB29-human insulin analog. 47. The composition of Claim 42, wherein the derivatized protein is fatty acid-acylated AspB28-human insulin analog. 48. The composition of Claim l, wherein the mole ratio between the protein and the derivatized protein is from about 1:9 to about 9:1. 49. The composition of Claim 48, wherein the ratio is from about 1:3 to about 3:1. 50. The composition of Claim 48, wherein the ratio is from about 1:9 to about 1:1. 51. The composition of Claim 1, wherein the protein is insulin. 52. The composition of Claim 1, wherein the protein is an insulin analog. 53. The composition of Claim 52, wherein the protein is a monomeric insulin analog. 54. A suspension formulation, comprising an insoluble phase and a solution phase, wherein the insoluble phase comprises the insoluble composition of Claim 1, and the solution phase comprises an aqueous solvent. 55. The suspension formulation of Claim 54, wherein the solution phase further comprises a phenolic preservative at a concentration of about 0.5 mg per mL to about 6 mg per mL of solution, a pharmaceutically acceptable buffer, and an isotonicity agent. 56. The suspension formulation of Claim 54, wherein the solution phase further comprises insulin, an insulin analog, a derivatized insulin, or a derivatized insulin analog. 57. The suspension formulation of Claim 56, wherein the solution phase comprises insulin. 58. The suspension formulation of Claim 56, wherein the solution phase comprises derivatized insulin. 59. The suspension formulation of Claim 56, wherein the solution phase comprises an insulin analog. 60. The suspension formulation of Claim 56, wherein the insulin analog is a monomeric insulin analog. 61. The suspension formulation of Claim 56, wherein the insulin analog is LysB28,ProB29-human insulin analog. 62. The suspension formulation of Claim 56, wherein the insulin analog is AspB28-human insulin analog. 63. The suspension formulation of Claim 54, wherein the solution phase further comprises a protein selected from insulin and insulin analogs and a derivatized protein selected from derivatized insulin and derivatized insulin analogs. 64. The suspension formulation of Claim 63 wherein the protein in the solution phase is the same protein that is in the insoluble phase, and wherein the derivatized protein in the solution phase is the same derivatized protein that is in the insoluble phase. 65. The suspension formulation of Claim 54, wherein the insoluble phase consists essentially of an amorphous precipitate. 66. The suspension formulation of Claim 54, wherein the insoluble phase consists essentially of a microcrystal. 67. The suspension formulation of Claim 54, wherein the insoluble phase consists of a mixture of amorphous precipitate and microcrystal. 68. The suspension formulation of Claim 54, wherein the solution phase further comprises zinc and protamine, wherein the ratio of zinc to total protein in the suspension formulation is from about 5 to about 7 mole of zinc atoms per mole of total protein, and the ratio of protamine to total protein in the suspension formulation is from about 0.25 mg to about 0.5 mg per mg of total protein. 69. A method of treating diabetes comprising administering the composition of Claim 1 to a patient in need thereof in a quantity sufficient to regulate blood glucose levels in the patient. 70. A method of treating hyperglycemia comprising administering the composition of Claim 54 to a patient in need thereof in a quantity sufficient to regulate blood glucose levels in the patient. 71. A hybrid hexamer composition, comprising six monomers and zinc, wherein at least one monomer is selected from the group consisting of insulin, insulin analogs, and proinsulins, and at least one monomer is selected from the group consisting of derivatized insulin, derivatized insulin analogs, and derivatized proinsulins. 72. A mixed hexamer composition, comprising zinc protein hexamers and zinc derivatized protein hexamers, wherein the zinc protein hexamers comprise zinc and a protein selected from the group consisting of insulin, insulin analogs, and proinsulins, and wherein the zinc derivatized protein hexamers comprise zinc and a derivatized protein selected from the group consisting of derivatized insulin, derivatized insulin analogs, and derivatized proinsulins. 73. A process for preparing the insoluble composition of Claim l comprising: a) dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers, and b) adding a complexing compound. 74. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will not permit the formation of hexamers, and b) adjusting the pH to between about 6.8 and about 7.8; and c) adding a complexing compound. 75. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers; b) separately, dissolving a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers; c) thoroughly mixing together the solutions from steps a) and b); and d) adding a complexing compound to the solution produced in step c). 76. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a hexamer-stabilizing compound, a divalent metal cation, and a complexing compound in an aqueous solvent, wherein the resulting solution has a pH at which precipitation does not occur; b) separately, dissolving a derivatized protein, a hexamer-stabilizing compound, a divalent metal cation, and a complexing compound in an aqueous solvent, wherein the resulting solution has a pH at which precipitation does not occur; c) thoroughly mixing together the solutions from steps a) and b); and d) adjusting the pH of the solution of step c) to a value at which precipitation occurs. 77. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, a divalent metal cation, and a complexing compound in an aqueous solvent, wherein the resulting solution has a pH at which precipitation does not occur; and b) adjusting the pH of the solution of step a) to a value at which precipitation occurs. 78. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation, in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing agent is added; b) adding a complexing compound; and c) adjusting the pH of the solution of step b) to a value at which precipitation occurs. 79. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added; b) separately, dissolving a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added; c) thoroughly mixing together the solutions from steps a) and b); d) adding complexing compound to the solution of step c) ; and e) adjusting the pH of the solution of step d) to a value at which precipitation occurs. 80. A process for preparing the insoluble composition of Claim l comprising: a) dissolving a protein, a protein derivative, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added; b) adjusting the pH of the solution of step a) to a value at which precipitation will occur when a complexing compound is added; and c) adding a complexing compound to the solution of step b). 81. A process for preparing the insoluble composition of Claim 1 comprising: a) dissolving a protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added; b) separately, dissolving a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent, wherein the resulting solution has a pH at which precipitation will not occur when a complexing compound is added; c) thoroughly mixing together the solutions from steps a) and b); d) adjusting the pH of the solution of step c) to a value at which precipitation will occur when a complexing compound is added; and e) adding a complexing compound to the solution of step d). 82. A process for preparing hybrid hexamers, comprising dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will permit the formation of hexamers. 83. A process for preparing hybrid hexamers, comprising: a) dissolving a protein, a derivatized protein, a hexamer-stabilizing compound, and a divalent metal cation in an aqueous solvent having a pH that will not permit the formation of hexamers, and b) adjusting the pH to between about 6.8 and about 7.8. An insoluble composition, comprising: a) a protein selected from the group consisting of insulin, insulin analog, and proinsulin; b) a derivatized protein selected from the group consisting of derivatized insulin, derivatized insulin analog, and derivatized proinsulin; c) a complexing compound; d) a hexamer-stabilizing compound; and e) a divalent metal cation.