4.6 Article

Current trends in α-helical membrane protein crystallization: An update

期刊

PROTEIN SCIENCE
卷 21, 期 9, 页码 1358-+

出版社

WILEY-BLACKWELL
DOI: 10.1002/pro.2122

关键词

membrane proteins; crystallization; crystallization additives

资金

  1. Medical Research Council (MRC) [G0900399]
  2. Medical Research Council [G0900399] Funding Source: researchfish
  3. MRC [G0900399] Funding Source: UKRI

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a-Helical membrane proteins (MPs) are the targets for many pharmaceutical drugs and play important roles in human physiology. In recent years, significant progress has been made in determining their atomic structure using X-ray crystallography. However, a major bottleneck in MP crystallography still remains, namely, the identification of conditions that give crystals that are suitable for structural determination. In 2008, we undertook an analysis of the crystallization conditions for 121 a-helical MPs to design a rationalized sparse matrix crystallization screen, MemGold. We now report an updated analysis that includes a further 133 conditions. The results reveal the current trends in a-helical MP crystallization with notable differences since 2008. The updated information has been used to design new crystallization and additive screens that should prove useful for both initial crystallization scouting and subsequent crystal optimization.

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