Merging In-Solution X-ray and Neutron Scattering Data Allows Fine Structural Analysis of Membrane-Protein Detergent Complexes.
Merging In-Solution X-ray and Neutron Scattering Data Allows Fine Structural Analysis of Membrane-Protein Detergent Complexes.
复制标题
合并溶液内 X 射线和中子散射数据可以对膜-蛋白质洗涤剂复合物进行精细结构分析。
DOI：
10.1021/acs.jpclett.8b01598
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Dias Mirandela G
中科院分区：
文献类型：
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作者：
Dias Mirandela G
In-solution small-angle X-ray and neutron scattering (SAXS/SANS) have become popular methods to characterize the structure of membrane proteins, solubilized by either detergents or nanodiscs. SANS studies of protein-detergent complexes usually require deuterium-labeled proteins or detergents, which in turn often lead to problems in their expression or purification. Here, we report an approach whose novelty is the combined analysis of SAXS and SANS data from an unlabeled membrane protein complex in solution in two complementary ways. First, an explicit atomic analysis, including both protein and detergent molecules, using the program WAXSiS, which has been adapted to predict SANS data. Second, the use of MONSA which allows one to discriminate between detergent head- and tail-groups in anab initioapproach. Our approach is readily applicable to any detergent-solubilized protein and provides more detailed structural information on protein–detergent complexes from unlabeled samples than SAXS or SANS alone.
