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Expression purification and crystallization of the C-terminal LRR domain of Streptococcus pyogenes protein 0843

机译:化脓性链球菌蛋白0843的C端LRR结构域的表达纯化和结晶

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摘要

Streptococcus pyogenes protein 0843 (Spy0843) is a recently identified protein with a potential adhesin function. Sequence analysis has shown that Spy0843 contains two leucine-rich repeat (LRR) domains that mediate interactions with the gp340 receptor. Here, the C-terminal LRR domain was overexpressed in Escherichia coli, purified and crystallized in the presence of 1.7–1.8 M ammonium sulfate pH 7.4 as precipitant. Data were collected from a single crystal to 1.59 Å resolution at 100 K at a synchrotron-radiation source. The crystal was found to belong to space group I41, with unit-cell parameters a = b = 121.4, c = 51.5 Å and one molecule in the asymmetric unit. Elucidation of the crystal structure will provide insights into the interactions of Spy0843 with the gp340 receptor and a better understanding of the role of Spy0843 in streptococcal infections.
机译:化脓性链球菌蛋白质0843(Spy0843)是最近鉴定出的具有潜在粘附素功能的蛋白质。序列分析表明,Spy0843包含两个富亮氨酸重复(LRR)域,介导与gp340受体的相互作用。在这里,C末端的LRR结构域在大肠杆菌中过表达,在1.7–1.8μM pH 7.4的硫酸铵存在下纯化和结晶。在同步辐射源中以100 K的分辨率从单晶以1.59resolutionÅ的分辨率收集数据。发现该晶体属于空间群I41,其晶胞参数a = b = 121.4,c = 51.5Å,并且一个分子位于不对称单元中。晶体结构的阐明将提供Spy0843与gp340受体相互作用的见解,并更好地了解Spy0843在链球菌感染中的作用。

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