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

被引:5
作者
Das, SK [1 ]
Sedelnikova, SE [1 ]
Baker, PJ [1 ]
Ruzheinikov, SN [1 ]
Foster, SJ [1 ]
Rice, DW [1 ]
机构
[1] Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷
关键词
D O I
10.1107/S0907444903024910
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom resolution and are suitable for structure determination.
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页码:166 / 168
页数:3
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