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

Watanabe, L.; Gava, L. M.; Angulo, Y.; Lomonte, B.; Arni, R. K.

Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/21989

Title:

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

Author(s):

Institution:

Universidade Estadual Paulista (UNESP)
Univ Costa Rica

ISSN:

1570-9639

Abstract:

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.

Issue Date:

1-Dec-2004

Citation:

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

Time Duration:

87-89

Publisher:

Elsevier B.V.

Keywords:

myotoxin
snake venom
phospholipase A(2)
Lysine-49
X-ray diffraction

Source:

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

URI:

Access Rights:

Acesso restrito

Type:

outro

Source:

http://repositorio.unesp.br/handle/11449/21989

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