Crystallization and preliminary X-ray diffraction characterization of RpfF, a key DSF synthase from Stenotrophomonas maltophilia.
Stenotrophomonas maltophilia has emerged as a critical nosocomial opportunistic pathogen in the last few years. It is resistant to many clinically useful antibiotics; hence, new ways of combatting this bacterium are essential. Diffusible signal factor (DSF) dependent quorum sensing is a major mechanism of virulence induction in S. maltophilia, with RpfF playing a key role in DSF biosynthesis. Inhibiting S. maltophilia RpfF (SmRpfF) function via small-molecule interference may constitute a new way of treating S. maltophilia infection. SmRpfF was therefore overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 148.51, c = 122.82 A, and diffracted to a resolution of 2.25 A.
Institute of Biochemistry, National Chung-Hsing University, Taichung 40227, Taiwan.
Xian Ya
XY
Lin
Shu Ju
SJ
Liao
Ko Hsin
KH
Chin
Hui Ling
HL
Shih
Gwan Han
GH
Shen
Andrew H J
AH
Wang
Shan Ho
SH
Chou
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D017434:Protein Structure, Tertiary; D053038:Quorum Sensing / Q000502:physiology; D020615:Stenotrophomonas maltophilia / Q000235:genetics*
D001426:Bacterial Proteins; D010450:Endopeptidases