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来自人类病原体金黄色葡萄球菌的II型NADH:醌氧化还原酶的表达、纯化、结晶及初步X射线衍射分析

Expression, purification, crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus.

作者信息

Rosário Ana Lúcia, Sena Filipa V, Batista Ana P, Oliveira Tânia F, Athayde Diogo, Pereira Manuela M, Brito José A, Archer Margarida

机构信息

Instituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Avenida República, 2780-157 Oeiras, Portugal.

出版信息

Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):477-82. doi: 10.1107/S2053230X15005178. Epub 2015 Mar 28.

Abstract

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.

摘要

近年来,II型NADH脱氢酶(NDH-IIs)已成为多种人类致病病原体的潜在药物靶点。在本研究中,来自革兰氏阳性人类病原体金黄色葡萄球菌的NDH-II酶在大肠杆菌中进行重组表达、纯化、结晶,并在波长为0.873 Å下收集了晶体学数据集。晶体属于正交空间群P212121,晶胞参数a = 81.8、b = 86.0、c = 269.9 Å,每个不对称单元包含四个单体,衍射分辨率为3.32 Å。已获得分子置换解,目前正在进行模型构建和精修。

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本文引用的文献

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