Purification, crystallization and preliminary X-ray analysis of human GIMAP2.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 6): 725-9, 2010 Jun 01.
Article
en En
| MEDLINE
| ID: mdl-20516611
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
GTP Fosfohidrolasas
/
Proteínas de la Membrana
Límite:
Humans
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2010
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Reino Unido