Crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9-and 1.45-A resolution

Takeda, AASdos Santos, J. I.Marcussi, S.Silveira, L. B.Soares, A. M.Fontes, MRM2014-05-202014-05-202004-06-01Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1699, n. 1-2, p. 281-284, 2004.1570-9639http://hdl.handle.net/11449/17577An acidic phospholipase A(2) (PLA(2)) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: alpha-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45- and 1.85-Angstrom resolution, respectively, for the complexes with alpha-tocopherol and p-bromophenacyl bromide. The crystals are not isomorphous with those of the native protein, suggesting the inhibitors binding was successful and changes in the quaternary structure may have occurred. (C) 2004 Elsevier B.V. All rights reserved.281-284engcrystallizationX-ray crystallographyacidic phospholipase A(2)Bothrops jararacussu venomalpha-tocopherolp-bromophenacyl bromideCrystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9-and 1.45-A resolutionArtigo10.1016/j.bbapap.2004.02.005WOS:000221807800030Acesso restrito