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dc.contributor.author
Gabrielsen, Mads
dc.contributor.author
Riboldi Tunnicliffe, Alan
dc.contributor.author
Ibáñez, Marina
dc.contributor.author
Griffiths, Kate
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Roe, Andrew J.
dc.contributor.author
Cooper, Alan
dc.contributor.author
Smith, Brian O.
dc.contributor.author
Córsico, Betina
dc.contributor.author
Kennedy, Malcolm W.
dc.date.available
2020-01-10T21:08:55Z
dc.date.issued
2012-08
dc.identifier.citation
Gabrielsen, Mads; Riboldi Tunnicliffe, Alan; Ibáñez, Marina; Griffiths, Kate; Roe, Andrew J.; et al.; Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section F-structural Biology And Crystallization Communications; 68; 8; 8-2012; 939-941
dc.identifier.issn
1744-3091
dc.identifier.uri
http://hdl.handle.net/11336/94415
dc.description.abstract
As-p18 is a fatty-acid-binding protein from the parasitic nematode Ascaris suum. Although it exhibits sequence similarity to mammalian intracellular fatty-acid-binding proteins, it contains features that are unique to nematodes. Crystals were obtained, but initial diffraction data analysis revealed that they were composed of a number of microdomains. Interpretable data could only be collected using a microfocus beamline with a beam size of 12 8 m.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ASCARIS SUUM
dc.subject
FATTY-ACID-BINDING PROTEINS
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MICROFOCUS BEAMLINES
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PARASITIC NEMATODES
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Métodos de Investigación en Bioquímica
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-04-26T18:20:40Z
dc.journal.volume
68
dc.journal.number
8
dc.journal.pagination
939-941
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Gabrielsen, Mads. University of Glasgow; Reino Unido
dc.description.fil
Fil: Riboldi Tunnicliffe, Alan. Australian Synchrotron; Australia
dc.description.fil
Fil: Ibáñez, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
dc.description.fil
Fil: Griffiths, Kate. University of Glasgow; Reino Unido
dc.description.fil
Fil: Roe, Andrew J.. University of Glasgow; Reino Unido
dc.description.fil
Fil: Cooper, Alan. University of Glasgow; Reino Unido
dc.description.fil
Fil: Smith, Brian O.. University of Glasgow; Reino Unido
dc.description.fil
Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
dc.description.fil
Fil: Kennedy, Malcolm W.. University of Glasgow; Reino Unido
dc.journal.title
Acta Crystallographica Section F-structural Biology And Crystallization Communications
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1107/S1744309112026553
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1107/S1744309112026553
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