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.
Department of Biology, University of Crete, PO Box 2208, GR-71003 Heraklion, Crete, Greece.
Katerina
K
Kefala
Dina
D
Kotsifaki
Mary
M
Providaki
Evangelia G
EG
Kapetaniou
Lawrence
L
Rahme
Michael
M
Kokkinidis
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D011550:Pseudomonas aeruginosa / Q000737:chemistry*; D014157:Transcription Factors / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; D014157:Transcription Factors