Rationalizing alpha-helical membrane protein crystallization.
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.
Newstead
Simon
S
Division of Molecular Biosciences, Membrane Protein Crystallography Group, Wolfson Laboratory, Imperial College London, London SW7 2AZ, United Kingdom.
Ferrandon
Sébastien
S
Iwata
So
S
D002021:Buffers; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D003902:Detergents / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012492:Salts / Q000737:chemistry
D002021:Buffers; D003902:Detergents; D008565:Membrane Proteins; D012492:Salts