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Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus

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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.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionFaciba FEB
dc.contributor.institutionCtr Univ Votuporanga
dc.date.accessioned2014-05-20T15:30:02Z
dc.date.available2014-05-20T15:30:02Z
dc.date.issued2000-12-01
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.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.format.extent1685-1687
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.doi10.1107/S0907444900015262
dc.identifier.fileWOS000165509100030.pdf
dc.identifier.issn0907-4449
dc.identifier.lattes2835029061696580
dc.identifier.urihttp://hdl.handle.net/11449/39487
dc.identifier.wosWOS:000165509100030
dc.language.isoeng
dc.publisherMunksgaard Int Publ Ltd
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallography
dc.rights.accessRightsAcesso aberto
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.typeArtigo
dcterms.licensehttp://journals.iucr.org/services/copyrightpolicy.html
dcterms.rightsHolderMunksgaard Int Publ Ltd
dspace.entity.typePublication
unesp.author.lattes2835029061696580
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt
unesp.departmentQuímica e Ciências Ambientais - IBILCEpt

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São José do Rio Preto - IBILCE - Instituto de Biociências, Letras e Ciências Exatas