Crystallization and preliminary X‐ray diffraction characterization of RpfF, a key DSF synthase from Stenotrophomonas maltophilia

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|65|10|1021-1023

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.65, Iss.10, 2009-10, pp. : 1021-1023

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Abstract

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 P41212 or P43212, with unit‐cell parameters a = b = 148.51, c = 122.82 Å, and diffracted to a resolution of 2.25 Å.

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