Rationalizing α-helical membrane protein crystallization

被引：116

作者：

Newstead, Simon ^{[1
]}

Ferrandon, Sebastien ^{[1
]}

Iwata, So ^{[1
,2
,3
]}

机构：

[1] Imperial Coll London, Wolfson Lab, Div Mol Biosci, MPC Grp, London SW7 2AZ, England

[2] Kyoto Univ, Fac Med, ERATO Human Receptor Crystallograph Project, Kyoto 6068501, Japan

[3] RIKEN, Genom Sci Ctr, Protein Res Grp, Yokohama, Kanagawa 2300045, Japan

来源：

PROTEIN SCIENCE | 2008年 / 17卷 / 03期

关键词：

membrane proteins; protein crystallization;

D O I：

10.1110/ps.073263108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：466 / 472

页数：7

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