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Crystallization and preliminary X-ray diffraction studies of an L-amino-acid oxidase from Lachesis muta venom

dc.contributor.authorUllah, Anwar [UNESP]
dc.contributor.authorMasood, Rehana [UNESP]
dc.contributor.authorSpencer, Patrick Jack
dc.contributor.authorMurakami, Mario Tyago
dc.contributor.authorArni, Raghuvir Krishnaswamy [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionIPEN
dc.contributor.institutionCtr Nacl Pesquisa Energia & Mat
dc.date.accessioned2015-03-18T15:55:03Z
dc.date.available2015-03-18T15:55:03Z
dc.date.issued2014-11-01
dc.description.abstractSnake-venom proteins form multi-component defence systems by the recruitment and rapid evolution of nonvenomous proteins and hence serve as model systems to understand the structural modifications that result in toxicity. l-Amino-acid oxidases (LAAOs) are encountered in a number of snake venoms and have been implicated in the inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. An l-amino-acid oxidase from Lachesis muta venom has been purified and crystallized. The crystals belonged to space group P2(1), with unit-cell parameters a = 66.05, b = 79.41, c= 100.52 angstrom, beta = 96.55 degrees. The asymmetric unit contained two molecules and the structure has been determined and partially refined at 3.0 angstrom resolution.en
dc.description.affiliationUNESP IBILCE, Dept Phys, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
dc.description.affiliationIPEN, Inst Pesquisas Energet & Nucl, Comissao Nacl Energia Nucl, BR-05508900 Sao Paulo, Brazil
dc.description.affiliationCtr Nacl Pesquisa Energia & Mat, Lab Nacl Biociencias LNBio, BR-13083970 Campinas, Brazil
dc.description.affiliationUnespUNESP IBILCE, Dept Phys, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipDAAD
dc.format.extent1556-1559
dc.identifierhttp://dx.doi.org/10.1107/S2053230X14017877
dc.identifier.citationActa Crystallographica Section F-structural Biology Communications. Hoboken: Wiley-blackwell, v. 70, p. 1556-1559, 2014.
dc.identifier.doi10.1107/S2053230X14017877
dc.identifier.issn1744-3091
dc.identifier.lattes9162508978945887
dc.identifier.orcid0000-0003-2460-1145
dc.identifier.urihttp://hdl.handle.net/11449/117062
dc.identifier.wosWOS:000344790900021
dc.language.isoeng
dc.publisherWiley-Blackwell
dc.relation.ispartofActa Crystallographica Section F-structural Biology Communications
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleCrystallization and preliminary X-ray diffraction studies of an L-amino-acid oxidase from Lachesis muta venomen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderWiley-Blackwell
dspace.entity.typePublication
unesp.author.lattes9162508978945887[5]
unesp.author.orcid0000-0003-3793-7393[1]
unesp.author.orcid0000-0002-0405-8010[4]
unesp.author.orcid0000-0003-2460-1145[5]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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