铜绿假单胞菌MvfR蛋白c端片段的纯化、结晶和初步x射线衍射分析。

IF 0.9 4区生物学 Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI:10.1107/S1744309112016661

Katerina Kefala, Dina Kotsifaki, Mary Providaki, Evangelia G Kapetaniou, Lawrence Rahme, Michael Kokkinidis

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引用次数: 11

摘要

lysr型转录调控因子MvfR通过转录调控多个群体感应调控的毒力因子，在铜绿假单胞菌致病性中起关键作用。该蛋白还控制致病性VI型分泌位点。MvfRC87是MvfR的242个残基c端片段，经大肠杆菌纯化结晶。利用同步辐射采集了x射线衍射数据，测定了晶体学参数。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein from Pseudomonas aeruginosa.

The LysR-type transcriptional regulator MvfR plays a critical role in Pseudomonas aeruginosa pathogenicity via the transcriptional regulation of multiple quorum-sensing-regulated virulence factors. The protein also controls pathogenic type VI secretion loci. MvfRC87, a 242-residue C-terminal segment of MvfR, was produced in Escherichia coli, purified and crystallized. X-ray diffraction data were collected using synchrotron radiation and crystallographic parameters were determined.

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来源期刊

Acta Crystallographica Section F-structural Biology and Crystallization Communications 生物-晶体学

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0.00%

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2-4 weeks

期刊介绍： Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.