首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytoplasmic domain of FlhB from Salmonella typhimurium
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Purification, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytoplasmic domain of FlhB from Salmonella typhimurium

机译:鼠伤寒沙门氏菌FlhB C端胞质域的纯化,结晶和初步X射线晶体学分析

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摘要

FlhB is a key protein in the regulation of protein export by the bacterial flagellar secretion system. It is composed of two domains: an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBc). FlhBc from Salmonella typhimurium has been successfully crystallized using the vapour-diffusion method. The crystals diffracted to 2.45 Å resolution and belonged to space group P42212, with unit-cell parameters a = b = 49.06, c = 142.94 Å. A selenomethionine-containing variant of FlhBc has also been crystallized in the same space group and was used for initial phase calculation by the multiwavelength anomalous dispersion (MAD) method.
机译:FlhB是细菌鞭毛分泌系统调节蛋白质输出的关键蛋白质。它由两个结构域组成:一个N端跨膜结构域和一个C端胞质结构域(FlhBc)。鼠伤寒沙门氏菌的FlhBc已使用蒸气扩散法成功结晶。晶体衍射至2.45Å的分辨率,属于空间群P42212,其晶胞参数a = b = 49.06,c = 142.94Å。含硒代蛋氨酸的FlhBc变体也已在相同的空间群中结晶,并通过多波长异常色散(MAD)方法用于初始相位计算。

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