Crystallization of the Lys49 PLA(2) homologue, myotoxin II, from the venom of Atropoides nummifer


Autoria(s): Watanabe, L.; Gava, L. M.; Angulo, Y.; Lomonte, B.; Arni, R. K.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/12/2004

Resumo

Myotoxin H, a Lys49 catalytically inactive phospholipase A(2) homologue from Atropoides nummifer venom, was purified, characterized and crystallized. The crystals belongs to the tetragonal system, space group P4(3)2(1)2, with unit cell parameters (a=b=68.66 and c=63.87 Angstrom). Diffraction data were collected to a resolution of 2.32 Angstrom. The crystal structure is currently being determined using molecular replacement techniques. (C) 2004 Elsevier B.V. All rights reserved.

Formato

87-89

Identificador

http://dx.doi.org/10.1016/j.bbapap.2004.09.006

Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1703, n. 1, p. 87-89, 2004.

1570-9639

http://hdl.handle.net/11449/21989

10.1016/j.bbapap.2004.09.006

WOS:000225621800011

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Biochimica et Biophysica Acta: Proteins and Proteomics

Direitos

closedAccess

Palavras-Chave #myotoxin #snake venom #phospholipase A(2) #Lysine-49 #X-ray diffraction
Tipo

info:eu-repo/semantics/article