Open AccessPurification, crystallization and preliminary crystallographic analysis of a GTP‐binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus
Author(s) -
Wu Hao,
Sun Lei,
Brouns Stan J. J.,
Fu Sheng,
Akerboom Jasper,
Li Xuemei,
Van Der Oost John
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107008500
Subject(s) - sulfolobus solfataricus , sulfolobus , crystallization , crystallography , archaea , gtp' , chemistry , biochemistry , enzyme , organic chemistry , gene
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 Å using a single cadmium‐incorporated crystal. The crystal form belongs to space group P 2 1 2 1 2 1 , with approximate unit‐cell parameters a = 65.0, b = 72.6, c = 95.9 Å and with a monomer in the asymmetric unit.