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

α‐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...

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Bibliographic Details
Published in:Protein science 2012-09, Vol.21 (9), p.1358-1365
Main Authors: Parker, Joanne L., Newstead, Simon
Format: Article
Language:English
Subjects:
Animals
Buffers
Chemical Precipitation
crystallization
Crystallization - methods
crystallization additives
Crystallography, X-Ray - methods
Detergents - chemistry
Humans
Hydrogen-Ion Concentration
membrane proteins
Protein Structure, Secondary
Proteins - chemistry
Salts - chemistry
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Summary:α‐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 α‐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 α‐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.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.2122