Entropy and surface engineering in protein crystallization.

摘要: Protein crystallization remains a key limiting step in the characterization of atomic structures proteins and their complexes by X-ray diffraction methods. Current data indicate that standard screening procedures applied to soluble well folded prokaryotic yield crystals with an ∼20% success rate for eukaryotic this figure may be significantly lower. is predominantly dependent on entropic effects driving force appears release ordered water from sites crystal contacts. This countered cost ordering protein molecules loss conformational freedom side chains involved Mutational surface engineering designed create patches low entropy thereby conducive formation contacts promises effective tool allowing direct enhancement macromolecular crystallization.