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

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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; GIMAP21–260) 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 GIMAP221–260 and GDP‐bound GIMAP21–234 crystallized in space group P212121 and the crystals diffracted X‐rays to 2.9 and 1.7 Å resolution, respectively. GTP‐bound GIMAP21–234 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.
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Keywords: GIMAP2; GTPase of immunity‐associated proteins; IMAP2

Document Type: Research Article

Affiliations: Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, 13125 Berlin, Germany

Publication date: June 1, 2010

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