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

Purification, crystallization and preliminary X‐ray diffraction analysis of the C‐terminal... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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References (8)

Publisher
Wiley
Copyright
International Union of Crystallography, 2012
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309112016661
pmid
22684073
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Acta Crystallographica Section FWiley

Published: Jun 1, 2012

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