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

Xian Ya Lin; Shu Ju Liao; Ko Hsin Chin; Hui Ling Shih; Gwan Han Shen; Andrew H.J. Wang; Shan Ho Chou

doi:10.1107/S1744309109033156

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

Xian Ya Lin, Shu Ju Liao, Ko Hsin Chin, Hui Ling Shih, Gwan Han Shen, Andrew H.J. Wang, Shan Ho Chou

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	1021-1023
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	65
Issue number	10
DOIs	https://doi.org/10.1107/S1744309109033156
Publication status	Published - 2009
Externally published	Yes

Keywords

DFS synthase
RpfF
Stenotrophomonas maltophilia
Structural genomics

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309109033156

Cite this

Lin, X. Y., Liao, S. J., Chin, K. H., Shih, H. L., Shen, G. H., Wang, A. H. J., & Chou, S. H. (2009). Crystallization and preliminary X-ray diffraction characterization of RpfF, a key DSF synthase from Stenotrophomonas maltophilia. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(10), 1021-1023. https://doi.org/10.1107/S1744309109033156

Crystallization and preliminary X-ray diffraction characterization of RpfF, a key DSF synthase from Stenotrophomonas maltophilia. / Lin, Xian Ya; Liao, Shu Ju; Chin, Ko Hsin et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 10, 2009, p. 1021-1023.

Research output: Contribution to journal › Article › peer-review

Lin, XY, Liao, SJ, Chin, KH, Shih, HL, Shen, GH, Wang, AHJ & Chou, SH 2009, 'Crystallization and preliminary X-ray diffraction characterization of RpfF, a key DSF synthase from Stenotrophomonas maltophilia', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 65, no. 10, pp. 1021-1023. https://doi.org/10.1107/S1744309109033156

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title = "Crystallization and preliminary X-ray diffraction characterization of RpfF, a key DSF synthase from Stenotrophomonas maltophilia",

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 {\AA}, and diffracted to a resolution of 2.25 {\AA}.",

keywords = "DFS synthase, RpfF, Stenotrophomonas maltophilia, Structural genomics",

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AU - Lin, Xian Ya

AU - Liao, Shu Ju

AU - Chin, Ko Hsin

AU - Shih, Hui Ling

AU - Shen, Gwan Han

AU - Wang, Andrew H.J.

AU - Chou, Shan Ho

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

Abstract

Keywords

ASJC Scopus subject areas

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