首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and initial X-ray diffraction study of the three PASTA domains of the Ser/Thr kinase Stk1 from the human pathogen Staphylococcus aureus
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Crystallization and initial X-ray diffraction study of the three PASTA domains of the Ser/Thr kinase Stk1 from the human pathogen Staphylococcus aureus

机译:人类病原体金黄色葡萄球菌的Ser / Thr激酶Stk1的三个PASTA结构域的结晶和初始X射线衍射研究

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摘要

PASTA subunits (∼70 amino acids) are specific to bacterial serine/threonine kinases and to penicillin-binding proteins (PBPs) and are involved in the synthesis of peptidoglycan. The human pathogen Staphylococcus aureus contains a serine/threonine kinase, Stk1, which plays a major role in virulence. A recombinant His-tagged portion of the extracellular domain of Stk1 containing three PASTA subunits has been crystallized using zinc sulfate as a crystallizing agent. The crystals belonged to the tetragonal space group P4122, with unit-cell parameters a = 68.0, b = 68.0, c = 158.1 Å. Structure determination by the MAD method is now in progress.
机译:PASTA亚基(约70个氨基酸)对细菌的丝氨酸/苏氨酸激酶和青霉素结合蛋白(PBP)具有特异性,并参与肽聚糖的合成。人类病原体金黄色葡萄球菌含有丝氨酸/苏氨酸激酶Stk1,在毒力中起主要作用。 Stk1的胞外域的重组His标记的部分包含三个PASTA亚基已使用硫酸锌作为结晶剂进行了结晶。晶体属于四边形空间群P4122,单位晶胞参数a = 68.0,b = 68.0,c = 158.1Å。现在正在通过MAD方法确定结构。

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