Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction

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dc.catalogadordfo
dc.contributor.authorPangborn, Walter
dc.contributor.authorErman, Mary
dc.contributor.authorLi, Naiyin
dc.contributor.authorBurkhart, Brian M.
dc.contributor.authorPletnev, Vladimir Z.
dc.contributor.authorDuax, William L.
dc.contributor.authorGutiérrez Ilabaca, Rodrigo Antonio
dc.contributor.authorPeirano, Alessandra
dc.contributor.authorEyzaguirre, Jaime
dc.contributor.authorThiel, Daniel J.
dc.contributor.authorGhosh, Debashis
dc.date.accessioned2024-01-31T12:39:21Z
dc.date.available2024-01-31T12:39:21Z
dc.date.issued1996
dc.description.abstractAcetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9 Å, b = 61.0 Å, c = 72.5 Å.
dc.fuente.origenORCID-ene24
dc.identifier.doi10.1002/(SICI)1097-0134(199604)24:4<523
dc.identifier.urihttps://doi.org/10.1002/(SICI)1097-0134(199604)24:4<523
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/81087
dc.information.autorucFacultad de Ciencias Biológicas; Gutiérrez Ilabaca, Rodrigo Antonio; 0000-0002-5961-5005; 86782
dc.issue.numero4
dc.language.isoen
dc.nota.accesoContenido parcial
dc.pagina.final524
dc.pagina.inicio523
dc.revistaProteins: Structure, Function, and Bioinformatics
dc.rightsacceso restringido
dc.subjectEsterase
dc.subjectCrystallography
dc.subjectCrystallization
dc.subjectSynchrotron radiation
dc.subject.ddc610
dc.subject.deweyMedicina y saludes_ES
dc.titleCharacterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction
dc.typeartículo
dc.volumen24
sipa.codpersvinculados86782
sipa.trazabilidadWOS;05-06-2021
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