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首页> 外文期刊>Crystallography reports >In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering
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In situ study of the state of lysozyme molecules at the very early stage of the crystallization process by small-angle X-ray scattering

机译：通过小角度X射线散射原位研究溶菌酶分子在结晶过程的早期阶段的状态

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摘要

The molecular state of hen egg white lysozyme in solution has been studied by small-angle X-ray scattering (SAXS) combined with molecular simulation. The addition of a precipitant is shown to change the state of the protein molecules in solution. The SAXS data were processed using the constructed models of different oligomers. Under the crystallization conditions, lysozyme is shown to be present in solution as monomers (96.0%), dimers (1.9%), and octamers (2.1%), whereas tetramers and hexamers are not found. The modeled structure of the octamer is not consistent with the commonly accepted unit cell containing eight lysozyme molecules. Meanwhile, the modeled octamers are well-fitted to the crystal structure and can serve as building blocks in the course of crystal growth.
机译：通过小角度X射线散射（SAXS）结合分子模拟研究了鸡蛋清溶菌酶在溶液中的分子状态。已显示添加沉淀剂会改变溶液中蛋白质分子的状态。使用不同寡聚物的构建模型处理SAXS数据。在结晶条件下，溶菌酶以单体（96.0％），二聚体（1.9％）和八聚体（2.1％）的形式存在于溶液中，但未发现四聚体和六聚体。八聚体的建模结构与普遍接受的包含八个溶菌酶分子的单位细胞不一致。同时，建模的八聚体非常适合晶体结构，并且可以作为晶体生长过程中的基础。

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