Crystallization and preliminary X-ray crystallographic analysis of the heterodimeric crotoxin complex and the isolated subunits crotapotin and phospholipase A(2)


Autoria(s): Santos, K. F.; Murakami, M. T.; Cintra, A. C. O.; Toyama, M. H.; Marangoni, S.; Forrer, V. P.; Brandao Neto, J. R.; Polikarpov, I.; Arni, R. K.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/04/2007

Resumo

Crotoxin, a potent neurotoxin from the venom of the South American rattlesnake Crotalus durissus terrificus, exists as a heterodimer formed between a phospholipase A(2) and a catalytically inactive acidic phospholipase A(2) analogue (crotapotin). Large single crystals of the crotoxin complex and of the isolated subunits have been obtained. The crotoxin complex crystal belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 38.2, b = 68.7, c = 84.2 angstrom, and diffracted to 1.75 angstrom resolution. The crystal of the phospholipase A(2) domain belongs to the hexagonal space group P6(1)22 (or its enantiomorph P6(5)22), with unit-cell parameters a = b = 38.7, c = 286.7 angstrom, and diffracted to 2.6 angstrom resolution. The crotapotin crystal diffracted to 2.3 angstrom resolution; however, the highly diffuse diffraction pattern did not permit unambiguous assignment of the unit-cell parameters.

Formato

287-290

Identificador

http://dx.doi.org/10.1107/S1744309107006719

Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 63, p. 287-290, 2007.

1744-3091

http://hdl.handle.net/11449/21999

10.1107/S1744309107006719

WOS:000245505800008

Idioma(s)

eng

Publicador

Blackwell Publishing

Relação

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Direitos

closedAccess

Tipo

info:eu-repo/semantics/article