Enhanced protein crystallization around the metastable critical point
Theor. Chem. Acc. , Volume 101 p. 205- 208
We report on a computer-simulation study of homogeneous crystal nucleation in a model for globular proteins. We find that the presence of a metastable vapour-liquid critical point drastically changes the pathway for the formation of a critical nucleus. But what is more important, the large density fluctuations near the critical point also lowers the free-energy barrier to nucleation and hence increases the nucleation rate. As the location of the vapour-liquid critical point can be controlled by changing the solvent conditions, our simulation results suggest a guided approach to protein crystallization.