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Updated: Aug 15, 2026

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments
Published on: February 4, 2021
Protein crystal nucleation: is the pair interaction potential the primary determinant of kinetics?
Venkateswarlu Bhamidi1, Sasidhar Varanasi, Constance A Schall
1Department of Chemical & Environmental Engineering, University of Toledo, 2801 W. Bancroft St., Toledo, OH 43606, USA.
Abstract:
Fundamental understanding of protein crystal nucleation facilitates crystallization of biological macromolecules for structure determination and control of crystal size distribution. In the studies presented here, nucleation kinetics of hen egg-white lysozyme crystals were measured at solution conditions that exhibited equal solubility by adjusting pH, temperature, or sodium chloride concentration. It was observed that solution conditions that lead to equal solubility resulted in equal nucleation rates and hence kinetic parameters. Since the solubility of globular proteins correlates with the osmotic second virial coefficient, B(22), an integral measure of the protein pair interaction potential, this observation indicates that the protein pair interaction plays a key role in determining nucleation kinetic parameters.
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