Expression, purification, crystallization and preliminary crystallographic analysis of a putative GTP-binding protein, YsxC, from Bacillus subtilis

Das, S. K. ; Sedelnikova, S. E. ; Baker, P. J. ; Ruzheinikov, S. N. ; Foster, S. J. ; Rice, D. W. (2004) Expression, purification, crystallization and preliminary crystallographic analysis of a putative GTP-binding protein, YsxC, from Bacillus subtilis Acta Crystallographica Section D, D60 (1). pp. 166-168. ISSN 0907-4449

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Official URL: http://scripts.iucr.org/cgi-bin/paper?S09074449030...

Related URL: http://dx.doi.org/10.1107/S0907444903024910

Abstract

Bacillus subtilis YsxC has been putatively identified as a member of the GTP-binding protein family. Gene-knockout/deletion analysis has suggested that this protein is essential for survival of the microorganism and hence may represent a target for the development of a novel anti-infective agent. The B. subtilis ysxC gene was cloned and the protein was overexpressed in Escherichia coli and subsequently purified. Using hanging-drop vapour-diffusion crystallization techniques, two different crystal forms of YsxC were obtained in the presence and absence of GDP and which have one and two copies of YsxC in the asymmetric unit, respectively. Both crystal forms diffract to beyond 2.0 Å resolution and are suitable for structure determination.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:GDP; GTP-binding Protein; YsxC; GTPase; Bacillus subtilis
ID Code:63476
Deposited On:29 Sep 2011 04:23
Last Modified:29 Sep 2011 04:23

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