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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain
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Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain

机译:结核分枝杆菌DNA回旋酶ATPase结构域的纯化,结晶和初步X射线晶体学研究

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摘要

Mycobacterium tuberculosis DNA gyrase, a nanomachine involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target of fluoroquinolones in the treatment of tuberculosis. The ATPase domain provides the energy required for catalysis by ATP hydrolysis. Two constructs corresponding to this 43 kDa domain, Mtb-GyrB47(C1) and Mtb-GyrB47(C2), have been overproduced, purified and crystallized. Diffraction data were collected from three crystal forms. The crystals belonged to space groups P1 and P2(1) and diffracted to resolutions of 2.9 and 3.3 angstrom, respectively.
机译:结核分枝杆菌DNA促旋酶是一种参与DNA拓扑结构调控的纳米机器,是该生物中存在的唯一II型拓扑异构酶,因此是氟喹诺酮类药物在结核病治疗中的唯一靶标。 ATPase结构域提供了ATP水解催化所需的能量。对应于此43 kDa结构域的两个构建体Mtb-GyrB47(C1)和Mtb-GyrB47(C2)已被过量生产,纯化和结晶。从三种晶体形式收集衍射数据。晶体属于空间群P1和P2(1),分别衍射到2.9和3.3埃的分辨率。

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