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Curr Opin Struct Biol. 2009 Aug;19(4):449-57. doi: 10.1016/j.sbi.2009.04.008. Epub 2009 May 26.

Engineering of recombinant crystallization chaperones.

Author information

1
Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA. skoide@uchicago.edu

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.

PMID:
19477632
PMCID:
PMC2736338
DOI:
10.1016/j.sbi.2009.04.008
[Indexed for MEDLINE]
Free PMC Article
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