Correlation of second virial coefficients and solubilities useful in protein crystal growth

Abstract The osmotic second virial coefficient, B , is a dilute solution parameter, so one may wonder what relationships exist among B and the many facets of protein crystal growth (PCG). In particular, knowledge of how a protein's solubility ( S ) depends on solution variables such as temperature, pH and ionic strength is very useful for finding optimum conditions for the PCG experiment. In this work, a correlation between the second virial coefficient and protein solubility is shown for ovalbumin and lysozyme solutions. The data presented suggest significant correlation between B and S as a function of crystallizing salt type and concentration, pH and temperature. The data are presented both in graphical and tabular form so that it maybe useful to researchers desiring to develop and test detailed models for protein interactions.

[1]  Charles F. Zukoski,et al.  Protein interactions and crystallization , 1996 .

[2]  W. Grubb.  Ionic Migration in Ion-exchange Membranes , 1959 .

[3]  C. Stoscheck,et al.  Quantitation of protein. , 1990, Methods in enzymology.

[4]  F. Rosenberger,et al.  Interactions in undersaturated and supersaturated lysozyme solutions: Static and dynamic light scattering results , 1995 .

[5]  J. Drenth,et al.  The interaction energy between two protein molecules related to physical properties of their solution and their crystals and implications for crystal growth , 1995 .

[6]  Charles Tanford,et al.  Physical Chemistry of Macromolecules , 1961 .

[7]  Zamora,et al.  Phase behavior of small attractive colloidal particles. , 1996, Physical review letters.

[8]  F. Boué,et al.  Lysozyme-lysozyme interactions in under- and super-saturated solutions: a simple relation between the second virial coefficients in H2O and D2O , 1997 .

[9]  A. Ducruix,et al.  Relative effectiveness of various ions on the solubility and crystal growth of lysozyme. , 1989, The Journal of biological chemistry.

[10]  P. Kratochvíl.  Classical Light Scattering from Polymer Solutions , 1987 .

[11]  R. J. Baxter.  Percus-Yevick Equation for Hard Spheres with Surface Adhesion , 1968 .

[12]  A George,et al.  Predicting protein crystallization from a dilute solution property. , 1994, Acta crystallographica. Section D, Biological crystallography.

[13]  Marc L. Pusey,et al.  The solubility of the tetragonal form of hen egg white lysozyme from pH 4.0 to 5.4 , 1991 .

[14]  W. G. McMillan,et al.  The Statistical Thermodynamics of Multicomponent Systems , 1945 .

[15]  R. Giegé,et al.  Diagnostic of precipitant for biomacromolecule crystallization by quasi-elastic light-scattering. , 1990, Journal of molecular biology.

[16]  W. William Wilson,et al.  Laser scattering in a hanging drop vapor diffusion apparatus for protein crystal growth in a microgravity environment , 1992 .

[17]  Broide,et al.  Using phase transitions to investigate the effect of salts on protein interactions. , 1996, Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics.

[18]  J. Prausnitz,et al.  Thermodynamic properties of aqueous .alpha.-chymotrypsin solution from membrane osmometry measurements , 1992 .

[19]  E. T. White,et al.  Solubility of ovalbumin in ammonium sulfate solutions , 1996 .

[20]  Alexander McPherson,et al.  Preparation and analysis of protein crystals , 1982 .