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Published online before print January 24, 2008, 10.1110/ps.073263108
Protein Science (2008), 17:466-472. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Rationalizing {alpha}-helical membrane protein crystallization

Simon Newstead1, Sébastien Ferrandon1, and So Iwata1,2,3

1 Division of Molecular Biosciences, Membrane Protein Crystallography Group, Wolfson Laboratory, Imperial College London, London SW7 2AZ, United Kingdom
2 ERATO Human Receptor Crystallography Project, Kyoto University Faculty of Medicine, Kyoto 606-8501, Japan
3 Protein Research Group, RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan

(RECEIVED September 24, 2007; FINAL REVISION November 13, 2007; ACCEPTED November 15, 2007)

X-ray crystallography is currently the most successful method for determining the three-dimensional structure of membrane proteins. Nevertheless, growing the crystals required for this technique presents one of the major bottlenecks in this area of structural biology. This is especially true for the {alpha}-helical type membrane proteins that are of particular interest due to their medical relevance. To address this problem we have undertaken a detailed analysis of the crystallization conditions from 121 {alpha}-helical membrane protein structures deposited in the Protein Data Bank. This information has been analyzed so that the success of different parameters can be easily compared for different membrane protein families. Concurrent with this analysis, we also present the new sparse matrix crystallization screen MemGold.

Keywords: membrane proteins; protein crystallization


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