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dc.contributor.authorDias, MVB-
dc.contributor.authorEly, F.-
dc.contributor.authorCanduri, F.-
dc.contributor.authorPereira, J. F.-
dc.contributor.authorBasso, L. A.-
dc.contributor.authorPalma, Mario Sergio-
dc.contributor.authorde Azevedo, W. F.-
dc.contributor.authorSantos, D. S.-
dc.date.accessioned2014-05-20T13:54:20Z-
dc.date.accessioned2016-10-25T17:04:30Z-
dc.date.available2014-05-20T13:54:20Z-
dc.date.available2016-10-25T17:04:30Z-
dc.date.issued2004-11-01-
dc.identifierhttp://dx.doi.org/10.1107/S0907444904019869-
dc.identifier.citationActa Crystallographica Section D-biological Crystallography. Copenhagen: Blackwell Munksgaard, v. 60, p. 2003-2005, 2004.-
dc.identifier.issn0907-4449-
dc.identifier.urihttp://hdl.handle.net/11449/19411-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/19411-
dc.description.abstractThe enzymes of the shikimate pathway are potential targets for the development of new therapies because they are essential for bacteria but absent from mammals. The last step in this pathway is performed by chorismate synthase (CS), which catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate to chorismate. Optimization of crystallization trials allowed the crystallization of homogeneous recombinant CS from Mycobacterium tuberculosis (MtCS). The crystals of MtCS belong to space group P6(4)22 (or P6(2)22) and diffract to 2.8 Angstrom resolution, with unit-cell parameters a = b = 129.7, c = 156.8 Angstrom. There are two molecules in the asymmetric unit. Molecular-replacement trials were not sucessful. Heavy-atom derivative screening is in progress.en
dc.format.extent2003-2005-
dc.language.isoeng-
dc.publisherBlackwell Munksgaard-
dc.sourceWeb of Science-
dc.titleCrystallization and preliminary X-ray crystallographic analysis of chorismate synthase from Mycobacterium tuberculosisen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade Federal do Rio Grande do Sul (UFRGS)-
dc.contributor.institutionPontificia Univ Catolica Rio Grande do Sul-
dc.description.affiliationUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUFRGS, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisas TB Grp Microbiol Mol &, BR-91501970 Porto Alegre, RS, Brazil-
dc.description.affiliationUNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil-
dc.description.affiliationPontificia Univ Catolica Rio Grande do Sul, Inst Pesquisas Biomed, Ctr Pesquisas Biol Mol & Func, BR-90619900 Porto Alegre, RS, Brazil-
dc.description.affiliationUnespUNESP, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biosci, Dept Biol, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil-
dc.identifier.doi10.1107/S0907444904019869-
dc.identifier.wosWOS:000224595200012-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallography-
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