Logotipo do repositório
 

Publicação:
Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis venom

Carregando...
Imagem de Miniatura

Orientador

Coorientador

Pós-graduação

Curso de graduação

Título da Revista

ISSN da Revista

Título de Volume

Editor

Blackwell Publishing

Tipo

Artigo

Direito de acesso

Acesso restrito

Resumo

Zhaoermiatoxin, an Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA(2)-homologue family that possesses an arginine residue at position 49, probably arising from a secondary Lys49 -> Arg substitution that does not alter the catalytic inactivity towards phospholipids. Like other Lys49 PLA(2) homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA(2) catalytic activity. A single crystal with maximum dimensions of 0.2 x 0.2 x 0.5 mm was used for X-ray diffraction data collection to a resolution of 2.05 angstrom using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P6(4), with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 angstrom.

Descrição

Palavras-chave

Idioma

Inglês

Como citar

Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 63, p. 605-607, 2007.

Itens relacionados

Financiadores

Unidades

Departamentos

Cursos de graduação

Programas de pós-graduação