Purification, crystallization and preliminary X-ray analysis of human GIMAP2

Item Type:	Article
Title:	Purification, crystallization and preliminary X-ray analysis of human GIMAP2
Creators Name:	Schwefel, D. and Froehlich, C. and Daumke, O.
Abstract:	GTPases of immunity-associated proteins (GIMAPs) are important regulators of T-cell death and survival. Here, the crystallization and data collection of three GIMAP2 constructs in various nucleotide-loaded states is described. Selenomethionine-substituted carboxy-terminally truncated GIMAP2 (amino-acid residues 1-260; GIMAP2(1-260)) in the nucleotide-free form crystallized in space group P2(1)2(1)2(1) and the crystals diffracted X-rays to 1.5 A resolution. The phase problem was solved using the single anomalous dispersion (SAD) protocol. GDP-bound GIMAP2(21-260) and GDP-bound GIMAP2(1-234) crystallized in space group P2(1)2(1)2(1) and the crystals diffracted X-rays to 2.9 and 1.7 A resolution, respectively. GTP-bound GIMAP2(1-234) crystallized in space group C222(1) and the crystals diffracted to 1.9 A resolution. These results will allow a detailed structural analysis of GIMAP2, which will provide insight into the architecture and function of the GIMAP family.
Keywords:	GTPase of Immunity-Associated Proteins, GIMAP2, IMAP2
Source:	Acta Crystallographica Section F
ISSN:	1744-3091
Publisher:	International Union of Crystallography
Volume:	66
Number:	6
Page Range:	725-729
Date:	1 June 2010
Official Publication:	https://doi.org/10.1107/S174430911001537X
PubMed:	View item in PubMed

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