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. 2007 Apr 1;63(Pt 4):287-90.
doi: 10.1107/S1744309107006719. Epub 2007 Mar 12.

Crystallization and preliminary X-ray crystallographic analysis of the heterodimeric crotoxin complex and the isolated subunits crotapotin and phospholipase A2

K F Santos  1 , M T Murakami, A C O Cintra, M H Toyama, S Marangoni, V P Forrer, J R Brandão Neto, I Polikarpov, R K Arni
Affiliations

Crystallization and preliminary X-ray crystallographic analysis of the heterodimeric crotoxin complex and the isolated subunits crotapotin and phospholipase A2

K F Santos et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

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 A, and diffracted to 1.75 A 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 A, and diffracted to 2.6 A resolution. The crotapotin crystal diffracted to 2.3 A resolution; however, the highly diffuse diffraction pattern did not permit unambiguous assignment of the unit-cell parameters.

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Figures

Figure 1
Figure 1
Photomicrographs of (a) PLA2 and (b) crotapotin crystals.
See this image and copyright information in PMC

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