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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleCrystallization and preliminary X-ray diffraction analysis of Q4DV70 from Trypanosoma cruzi, a hypothetical protein with a putative thioredoxin domainpt_BR
dc.contributor.authordos Santos, CRpt_BR
dc.contributor.authorFessel, MRpt_BR
dc.contributor.authorVieira, LDpt_BR
dc.contributor.authorKrieger, MApt_BR
dc.contributor.authorGoldenberg, Spt_BR
dc.contributor.authorGuimaraes, BGpt_BR
dc.contributor.authorZanchin, NITpt_BR
dc.contributor.authorBarbosa, JARGpt_BR
unicamp.authordos Santos, Camila Ramos Fessel, Melissa Regina Vieira, Leandro de Carvalho Tonin Zanchin, Nilson Ivo Ribeiro Goncalves Barbosa, Joao Alexandre Brazilian Synchrotron Light Lab LNLS, Ctr Struct Mol Biol CeBiME, BR-13084971 Campinas, SP, Brazilpt_BR
unicamp.authordos Santos, Camila Ramos Ribeiro Goncalves Barbosa, Joao Alexandre Univ Estadual Campinas, Inst Biol, Campinas, SP, Brazilpt_BR
unicamp.authorKrieger, Marco Aurelio Goldenberg, Samuel Fiocruz MS, Inst Carlos Chagas, Curitiba, PR, Brazilpt_BR
unicamp.authorGuimaraes, Beatriz Gomes Synchrotron SOLEIL, St Aubin, Francept_BR
dc.subject.wosChaperone-like Activitypt_BR
dc.subject.wos3-dimensional Structurept_BR
dc.description.abstractQ4DV70 is annotated in the Trypanosoma cruzi CL Brener genome as a hypothetical protein with a predicted thioredoxin-like fold, although the catalytic cysteine residues that are conserved in typical oxidoreductases are replaced by serine residues. Gene- expression analysis indicates that this protein is differentially expressed during the T. cruzi life cycle, suggesting that it plays an important role during T. cruzi development. The gene coding for Q4DV70 was cloned and the protein was overexpressed in Escherichia coli with an N-terminal His tag. Purification of Q4DV70 was carried out by affinity and size-exclusion chromatography and the His tag was removed by TEV protease digestion. Crystals of Q4DV70 were grown using the sitting-drop vapour-diffusion method. A diffraction data set was collected to 1.50 angstrom resolution from a single crystal grown in 25% PEG 1500, 200 mM sodium thiocyanate pH 6.9, 10 mM phenol and 10% ethylene glycol. The crystal belonged to space group P2(1)2(1)2(1), with unitcell parameters a = 35.04, b = 50.32, c = 61.18 angstrom. The Q4DV70 structure was solved by molecular replacement using protein disulfide isomerase from yeast (PDB code 2b5e) as a search model. Initial refinement of the model indicated that the solution was correct. These data are being used for refinement of the model of
dc.relation.ispartofActa Crystallographica Section F-structural Biology And Crystallization Communicationspt_BR
dc.relation.ispartofabbreviationActa Crystallogr. F-Struct. Biol. Cryst. Commun.pt_BR
dc.publisherWiley-blackwell Publishing, Incpt_BR
dc.identifier.citationActa Crystallographica Section F-structural Biology And Crystallization Communications. Wiley-blackwell Publishing, Inc, v. 65, n. 641, n. 644, 2009.pt_BR
dc.sourceWeb of Sciencept_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipAssociacao Brasileira de Tecnologia de Luz Sincrotron (ABTLuS)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
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