Toward rational protein crystallization: A Web server for the design of crystallizable protein variants.

ABSTRACT: Growing well-diffracting crystals constitutes a serious bottleneck in structural biology. A recently proposed crystallization methodology for "stubborn crystallizers" is to engineer surface sequence variants designed to form intermolecular contacts that could support a crystal lattice. This approach relies on the concept of surface entropy reduction (SER), i.e., the replacement of clusters of flexible, solvent-exposed residues with residues with lower conformational entropy. This strategy minimizes the loss of conformational entropy upon crystallization and renders crystallization thermodynamically favorable. The method has been successfully used to crystallize more than 15 novel proteins, all stubborn crystallizers. But the choice of suitable sites for mutagenesis is not trivial. Herein,

SUBMITTER: Goldschmidt L 

PROVIDER: S-EPMC2203352 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature