Computer simulation of protein crystal growth using aggregates as the growth unit

Abstract

We present results of a computer simulation of protein crystal growth based on the Monte Carlo random process and surface kinetics of a growing crystal, which includes site-dependent detachment and migration, and site-independent attachment processes. The results indicate that, if only monomers are included in the attachment process, the simulation does not reproduce the experimentally observed rate of growth of lysozyme crystals at high supersaturation; however, using the same simulation parameters but allowing both monomers and aggregates to become attached to the crystal surface simulates the experimental results both at low and at high supersaturation. The results suggest possible influences of protein aggregates on the crystallization process.