Dependence of protein crystal stability on residue charge states and ion content of crystal solvent.

ABSTRACT: Protein crystallization is frequently induced by the addition of various precipitants, which directly affect protein solubility. In addition to organic cosolvents and long-chain polymers, salts belong to the most widely used precipitants in protein crystallography. However, despite such widespread usage, their mode of action at the atomistic level is still largely unknown. Here, we perform extensive molecular dynamics simulations of the villin headpiece crystal unit cell to examine its stability at different concentrations of sodium sulfate. We show that the inclusion of ions in crystal solvent at high concentration can prevent large rearrangements of the asymmetric units and a loss of symmetry of the unit cell without significantly affecting protein dynamics. Of importance, a similar resu

SUBMITTER: Kuzmanic A 

PROVIDER: S-EPMC3944895 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature