Crystallization of protein–protein complexes
Crystallization of protein–protein complexes
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DOI：
10.1107/s0021889802013973
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发表时间：
2002-12
影响因子：
6.1
通讯作者：
S. Radaev;P. Sun
中科院分区：
文献类型：
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作者：
S. Radaev;P. Sun
蛋白质-蛋白质复合物的结晶仍然是其结构表征的限速步骤。已知蛋白质-蛋白质复合物的结晶条件已经在蛋白质数据库和BMCD数据库中进行了调查。与非复合蛋白质相比，蛋白质-蛋白质复合物的结晶条件不太多样化，并且非常有利于（71%对27%）聚乙二醇（PEG）而不是硫酸铵或其他高盐结晶条件。结果表明，蛋白质复合物的稳定性限制了其可用的结晶构型空间。在此基础上，设计了一套稀疏矩阵筛选条件。
Crystallizing protein–protein complexes remains a rate-limiting step in their structure characterization. Crystallization conditions for the known protein–protein complexes have been surveyed in both the Protein Data Bank and the BMCD database. Compared with non-complexed proteins, crystallization conditions for protein–protein complexes are less diverse and heavily favor (71% versus 27%) polyethylene glycols (PEG) rather than ammonium sulfate or other high-salt crystallization conditions. The results suggest that the stability of protein complexes limits their available crystallization configuration space. Based on the survey, a set of sparse-matrix screen conditions was designed.