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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/39487
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dc.contributor.authorHonda, R. T.-
dc.contributor.authorDelatorre, P.-
dc.contributor.authorFadel, V-
dc.contributor.authorCanduri, F.-
dc.contributor.authorDellamano, M.-
dc.contributor.authorde Azevedo, W. F.-
dc.contributor.authorBonilla-Rodriguez, G. O.-
dc.date.accessioned2014-05-20T15:30:02Z-
dc.date.accessioned2016-10-25T18:05:25Z-
dc.date.available2014-05-20T15:30:02Z-
dc.date.available2016-10-25T18:05:25Z-
dc.date.issued2000-12-01-
dc.identifierhttp://dx.doi.org/10.1107/S0907444900015262-
dc.identifier.citationActa Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 56, p. 1685-1687, 2000.-
dc.identifier.issn0907-4449-
dc.identifier.urihttp://hdl.handle.net/11449/39487-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/39487-
dc.description.abstractHaemoglobin, the 'honorary enzyme' [Brunori (1999), Trends Biochem. Sci. 24, 158-161], constitutes a prime prototype for allosteric models. Here, the crystallization and preliminary X-ray analysis of haemoglobin I from the South American fish Brycon cephalus are reported. X-ray diffraction data have been collected to 2.5 Angstrom resolution using synchrotron radiation (LNLS). Crystals were determined to belong to the space group P6(1)22 and preliminary structural analysis revealed the presence of one dimer (alpha beta) in the asymmetric unit. The structure was determined using standard molecular-replacement techniques.en
dc.format.extent1685-1687-
dc.language.isoeng-
dc.publisherMunksgaard Int Publ Ltd-
dc.sourceWeb of Science-
dc.titleCrystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalusen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionFaciba FEB-
dc.contributor.institutionCtr Univ Votuporanga-
dc.description.affiliationUNESP, Inst Biociencias Letras & Ciências Exatas, Dept Quim & Geociencias, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP, Inst Biociencias Letras & Ciências Exatas, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationFaciba FEB, Dept Fis, BR-14783226 Barretos, SP, Brazil-
dc.description.affiliationCtr Univ Votuporanga, BR-15500030 Votuporanga, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biociencias Letras & Ciências Exatas, Dept Quim & Geociencias, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, Inst Biociencias Letras & Ciências Exatas, Dept Fis, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.identifier.doi10.1107/S0907444900015262-
dc.identifier.wosWOS:000165509100030-
dc.rights.accessRightsAcesso restrito-
dc.identifier.fileWOS000165509100030.pdf-
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallography-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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