Open AccessPurification, crystallization and preliminary X‐ray analysis of human GIMAP2
Author(s) -
Schwefel David,
Fröhlich Chris,
Daumke Oliver
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911001537x
Subject(s) - crystallization , resolution (logic) , crystallography , diffraction , nucleotide , gtp' , gtpase , chemistry , phase (matter) , x ray crystallography , materials science , physics , optics , biochemistry , computer science , gene , organic chemistry , artificial intelligence , enzyme
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 P 2 1 2 1 2 1 and the crystals diffracted X‐rays to 1.5 Å 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 P 2 1 2 1 2 1 and the crystals diffracted X‐rays to 2.9 and 1.7 Å resolution, respectively. GTP‐bound GIMAP2 1–234 crystallized in space group C 222 1 and the crystals diffracted to 1.9 Å resolution. These results will allow a detailed structural analysis of GIMAP2, which will provide insight into the architecture and function of the GIMAP family.