Engineering of Recombinant Crystallization Chaperones

Overview

Journal Curr Opin Struct Biol

Date 2009 May 30

PMID 19477632

Citations 88

Authors

Shohei Koide

Affiliations

Soon will be listed here.

Abstract

The preparation of diffraction quality crystals remains the major bottleneck in macromolecular X-ray crystallography. A crystallization chaperone is an auxiliary protein, such as fragments of monoclonal antibodies, that binds to and increases the crystallization probability of a target molecule of interest. Such chaperones reduce conformational heterogeneity, mask counterproductive surfaces while extending surfaces predisposed to forming crystal contacts, and provide phasing information. Crystallization chaperones generated using recombinant technologies have emerged as superior alternatives that increase the throughput and eliminate inherent limitations associated with antibody production by animal immunization and the hybridoma technology.

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