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.2014-05-202014-05-202007-04-01Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 63, p. 287-290, 2007.1744-3091http://hdl.handle.net/11449/21999Crotoxin, 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.287-290engCrystallization and preliminary X-ray crystallographic analysis of the heterodimeric crotoxin complex and the isolated subunits crotapotin and phospholipase A(2)Artigo10.1107/S1744309107006719WOS:000245505800008Acesso restrito91625089789458870000-0003-2460-1145