Newstead Simon, Ferrandon Sébastien, Iwata So
Division of Molecular Biosciences, Membrane Protein Crystallography Group, Wolfson Laboratory, Imperial College London, London SW7 2AZ, United Kingdom.
Protein Sci. 2008 Mar;17(3):466-72. doi: 10.1110/ps.073263108. Epub 2008 Jan 24.
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.
X射线晶体学是目前确定膜蛋白三维结构最成功的方法。然而,培养该技术所需的晶体是结构生物学这一领域的主要瓶颈之一。对于因其医学相关性而特别受关注的α-螺旋型膜蛋白来说尤其如此。为了解决这个问题,我们对蛋白质数据库中121个α-螺旋膜蛋白结构的结晶条件进行了详细分析。对这些信息进行了分析,以便能够轻松比较不同膜蛋白家族不同参数的成功率。在进行此分析的同时,我们还展示了新的稀疏矩阵结晶筛选方法MemGold。