Purification, crystallization and preliminary crystallographic studies of the TLDc domain of oxidation resistance protein 2 from zebrafish.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 67(Pt 10): 1253-6, 2011 Oct 01.
Article
en En
| MEDLINE
| ID: mdl-22102041
ABSTRACT
Cell metabolic processes are constantly producing reactive oxygen species (ROS), which have deleterious effects by triggering, for example, DNA damage. Numerous enzymes such as catalase, and small compounds such as vitamin C, provide protection against ROS. The TLDc domain of the human oxidation resistance protein has been shown to be able to protect DNA from oxidative stress; however, its mechanism of action is still not understood and no structural information is available on this domain. Structural information on the TLDc domain may therefore help in understanding exactly how it works. Here, the purification, crystallization and preliminary crystallographic studies of the TLDc domain from zebrafish are reported. Crystals belonging to the orthorhombic space group P2(1)2(1)2 were obtained and diffracted to 0.97 Å resolution. Selenomethionine-substituted protein could also be crystallized; these crystals diffracted to 1.1 Å resolution and the structure could be solved by SAD/MAD methods.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Pez Cebra
/
Proteínas Portadoras
/
Proteínas de Pez Cebra
Límite:
Animals
Idioma:
En
Año:
2011
Tipo del documento:
Article