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dc.contributor.authorFernández, Israel S.-
dc.contributor.authorStändker, Ludger-
dc.contributor.authorForssmann, Wolf Georg-
dc.contributor.authorGiménez-Gallego, Guillermo-
dc.contributor.authorRomero, Antonio-
dc.date.accessioned2012-12-20T09:05:11Z-
dc.date.available2012-12-20T09:05:11Z-
dc.date.issued2007-08-
dc.identifier.citationActa Crystallographica, Section F 63(8):669-672(2007)es_ES
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/10261/63366-
dc.description4 páginas, 6 figuras, 2 tablas -- PAGS nros. 669-672es_ES
dc.description.abstractHepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20 000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 Å resolution and data were collected to 99.6% completeness at 8.9 Å. The crystal belongs to space group P212121, with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 Å. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cellses_ES
dc.description.sponsorshipWe thank Professor K. Murray for providing plasmid pR1-11E. X-ray data collection was supported by BM14UK/ESRF, Grenoble and SRS, Daresbury. WST was supported by a Die NorKen Stiftung Visiting Fellowship and KLH is the recipient of the Darwin Trust Scholarshipes_ES
dc.language.isoenges_ES
dc.publisherInternational Union of Crystallographyes_ES
dc.rightsopenAccesses_ES
dc.subjecthepatitis B core particleses_ES
dc.subjectcryoprotectantes_ES
dc.subjecttemperature jumpes_ES
dc.subjectN-terminal fusiones_ES
dc.titleCrystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein familyes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1107/S1744309107031764-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1107/S1744309107031764es_ES
dc.identifier.pmid17671364-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.cerifentitytypePublications-
item.openairetypeartículo-
item.languageiso639-1en-
item.grantfulltextopen-
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