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Updated: Jul 25, 2026

Extraction of Venom and Venom Gland Microdissections from Spiders for Proteomic and Transcriptomic Analyses
Published on: November 3, 2014
Initial structural analysis of an alpha4beta4 C-type lectin from the venom of Crotalus durissus terrificus
M T Murakami1, L Watanabe, L M Gava
1Department of Physics, IBILCE/UNESP, R. Cristovão Colombo 2265, CEP 150054-000, São Jose do Rio Preto-SP, Brazil.
Abstract:
Convulxin, an alphabeta C-type lectin, is a potent platelet activator isolated from the venom of the South American rattlesnake Crotalus durissus terrificus. It is a 26.5 kDa alphabeta heterodimer consisting of two homologous disulfide-linked chains. The crystals belong to space group I4, with unit-cell parameters a = b = 131.61, c = 121.85 A, and diffraction data were collected to 2.7 A. The structure was solved by molecular replacement and the asymmetric unit contains two alphabeta heterodimers, each of which forms a disulfide-linked cyclic alpha(4)beta(4) tetramer in the unit cell. These alpha(4)beta(4) tetramers are stacked to form a large solvent channel.

