The stabilities of protein crystals.

ABSTRACT: We describe a model for protein crystallization equilibria. The model includes four terms, (1) protein translational entropy opposes crystallization, (2) proteins are attracted to each other by a nonelectrostatic contact free energy favoring crystallization, (3) proteins in the crystal repel each other but, to a greater extent, attract counterions sequestered in the crystal, which favors crystallization, and (4) the translational entropy of the counterions opposes their sequestration into the crystal, opposing crystallization. We treat the electrostatics using the nonlinear Poisson-Boltzmann equation, and we use unit cell information from native protein crystals to determine the boundary conditions. This model predicts the stabilities of protein crystals as functions of temperature, pH, an

SUBMITTER: Schmit JD 

PROVIDER: S-EPMC2919244 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature