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

janelia7_blocks-janelia7_biblio_header | block

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 2007 Mar 1;63:239-41. doi: 10.1107/S1744309107008500

Wu H, Sun L, Brouns SJ, Fu S, Akerboom J, Li X, van der Oost J

Note: Research in this publication was not performed at Janelia.

janelia7_blocks-janelia7_biblio_abstract | block

Abstract

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

node:body | entity_field

Main Menu (Mobile)- Block

Main Menu - Block

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

Note: Research in this publication was not performed at Janelia.

Abstract