Published January 1, 2011 | Version v1
Journal article Open

Crystallization and preliminary X-ray diffraction analysis of a class II phospholipase D from Loxosceles intermedia venom

  • 1. Univ Estadual Paulista, UNESP, Dept Fis, Ctr Multiusuario Inovacao Biomol, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
  • 2. Ctr Nacl Pesquisa Energia & Mat, LNBio, BR-13083970 Campinas, SP, Brazil
  • 3. Univ Fed Parana, Dept Biol Celular, BR-81531960 Curitiba, Parana, Brazil

Description

Phospholipases D are the major dermonecrotic component of Loxosceles venom and catalyze the hydrolysis of phospholipids, resulting in the formation of lipid mediators such as ceramide-1-phosphate and lysophosphatidic acid which can induce pathological and biological responses. Phospholipases D can be classified into two classes depending on their catalytic efficiency and the presence of an additional disulfide bridge. In this work, both wild-type and H12A-mutant forms of the class II phospholipase D from L. intermedia venom were crystallized. Wild-type and H12A-mutant crystals were grown under very similar conditions using PEG 200 as a precipitant and belonged to space group P12(1)1, with unit-cell parameters a = 50.1, b = 49.5, c = 56.5 angstrom, beta = 105.9 degrees. Wild-type and H12A-mutant crystals diffracted to maximum resolutions of 1.95 and 1.60 angstrom, respectively.

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