首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Expression purification crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus
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Expression purification crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus

机译:人类病原体金黄色葡萄球菌II型NADH:醌氧化还原酶的表达纯化结晶和初步X射线衍射分析

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摘要

In recent years, type II NADH dehydrogenases (NDH-IIs) have emerged as potential drug targets for a wide range of human disease causative agents. In this work, the NDH-II enzyme from the Gram-positive human pathogen Staphylococcus aureus was recombinantly expressed in Escherichia coli, purified, crystallized and a crystallographic data set was collected at a wavelength of 0.873 Å. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 81.8, b = 86.0, c = 269.9 Å, contained four monomers per asymmetric unit and diffracted to a resolution of 3.32 Å. A molecular-replacement solution was obtained and model building and refinement are currently under way.
机译:近年来,II型NADH脱氢酶(NDH-IIs)成为各种人类疾病致病因子的潜在药物靶标。在这项工作中,来自革兰氏阳性人类病原体金黄色葡萄球菌的NDH-II酶在大肠杆菌中重组表达,纯化,结晶,并收集了波长为0.873Å的晶体学数据集。晶体属于正交晶空间群P212121,单位晶胞参数a = 81.8,b = 86.0,c = 269.9Å,每个不对称单元包含四个单体,并衍射至3.32Å的分辨率。获得了分子置换解决方案,并且目前正在进行模型构建和完善。

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