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

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 P2₁2₁2₁ 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 P2₁2₁2₁ and the crystals diffracted X-rays to 2.9 and 1.7 Å resolution, respectively. GTP-bound GIMAP2^1-234 crystallized in space group C222₁ 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.