Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus

被引:3
|
作者
Wu, Hao
Sun, Lei
Brouns, Stan J. J.
Fu, Sheng
Akerboom, Jasper
Li, Xuemei [1 ]
van der Oost, John
机构
[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
[2] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Microbiol Lab, NL-6703 CT Wageningen, Netherlands
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词
D O I
10.1107/S1744309107008500
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
A predicted GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus, termed SsGBP, has been cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion technique in the presence of 0.05 M cadmium sulfate and 0.8 M sodium acetate pH 7.5. A single-wavelength anomalous dispersion data set was collected to a maximum resolution of 2.0 angstrom using a single cadmium-incorporated crystal. The crystal form belongs to space group P2(1)2(1)2(1), with approximate unit-cell parameters a = 65.0, b = 72.6, c = 95.9 angstrom and with a monomer in the asymmetric unit.
引用
收藏
页码:239 / 241
页数:3
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