Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the heterodimeric crotoxin complex and the isolated subunits crotapotin and phospholipase A 2
Author(s) -
Santos K. F.,
Murakami M. T.,
Cintra A. C. O.,
Toyama M. H.,
Marangoni S.,
Forrer V. P.,
Polikarpov I.,
Arni R. K.,
Brandão Neto J. R.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107006719
Subject(s) - orthorhombic crystal system , venom , phospholipase a2 , resolution (logic) , crystallography , crystallization , crystal structure , chemistry , diffraction , stereochemistry , biochemistry , enzyme , physics , optics , organic chemistry , artificial intelligence , computer science
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 P 2 1 2 1 2, with unit‐cell parameters a = 38.2, b = 68.7, c = 84.2 Å, and diffracted to 1.75 Å resolution. The crystal of the phospholipase A 2 domain belongs to the hexagonal space group P 6 1 22 (or its enantiomorph P 6 5 22), with unit‐cell parameters a = b = 38.7, c = 286.7 Å, and diffracted to 2.6 Å resolution. The crotapotin crystal diffracted to 2.3 Å resolution; however, the highly diffuse diffraction pattern did not permit unambiguous assignment of the unit‐cell parameters.