Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus.
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 A 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 A and with a monomer in the asymmetric unit.
Wu
Hao
H
Laboratory of Microbiology, Department of Agrotechnology and Food Sciences, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands.
Sun
Lei
L
Brouns
Stan J J
SJ
Fu
Sheng
S
Akerboom
Jasper
J
Li
Xuemei
X
van der Oost
John
J
D019843:Archaeal Proteins / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D019204:GTP-Binding Proteins / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D048229:Sulfolobus solfataricus / Q000737:chemistry* / Q000254:growth & development
D019843:Archaeal Proteins; D019204:GTP-Binding Proteins