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Engineering of recombinant crystallization chaperones

Authors :
Shohei Koide
Source :
Current Opinion in Structural Biology. 19:449-457
Publication Year :
2009
Publisher :
Elsevier BV, 2009.

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.

Details

ISSN :
0959440X
Volume :
19
Database :
OpenAIRE
Journal :
Current Opinion in Structural Biology
Accession number :
edsair.doi.dedup.....db1ced4a8fb4ab1d7fed7fa793837960
Full Text :
https://doi.org/10.1016/j.sbi.2009.04.008