Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline

Autores
Gabrielsen, Mads; Riboldi-Tunnicliffe, Alan; Ibáñez Shimabukuro, Marina; Griffiths, Kate; Roe, Andrew J.; Cooper, Alan; Smith, Brian O.; Córsico, Betina; Kennedy, Malcolm W.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Instituto de Investigaciones Bioquimicas de La Plata
Materia
Bioquímica
Ascaris suum
fatty-acid-binding proteins
microfocus beamlines
parasitic nematodes
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/84572
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/84572
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamlineGabrielsen, MadsRiboldi-Tunnicliffe, AlanIbáñez Shimabukuro, MarinaGriffiths, KateRoe, Andrew J.Cooper, AlanSmith, Brian O.Córsico, BetinaKennedy, Malcolm W.BioquímicaAscaris suumfatty-acid-binding proteinsmicrofocus beamlinesparasitic nematodesAs-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.Instituto de Investigaciones Bioquimicas de La Plata2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf939-941http://sedici.unlp.edu.ar/handle/10915/84572enginfo:eu-repo/semantics/altIdentifier/issn/1744-3091info:eu-repo/semantics/altIdentifier/doi/10.1107/S1744309112026553info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:07:57Zoai:sedici.unlp.edu.ar:10915/84572Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:07:57.837SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
title Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
spellingShingle Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
Gabrielsen, Mads
Bioquímica
Ascaris suum
fatty-acid-binding proteins
microfocus beamlines
parasitic nematodes
title_short Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
title_full Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
title_fullStr Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
title_full_unstemmed Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
title_sort Useable diffraction data from a multiple microdomain-containing crystal of Ascaris suum As-p18 fatty-acid-binding protein using a microfocus beamline
dc.creator.none.fl_str_mv Gabrielsen, Mads
Riboldi-Tunnicliffe, Alan
Ibáñez Shimabukuro, Marina
Griffiths, Kate
Roe, Andrew J.
Cooper, Alan
Smith, Brian O.
Córsico, Betina
Kennedy, Malcolm W.
author Gabrielsen, Mads
author_facet Gabrielsen, Mads
Riboldi-Tunnicliffe, Alan
Ibáñez Shimabukuro, Marina
Griffiths, Kate
Roe, Andrew J.
Cooper, Alan
Smith, Brian O.
Córsico, Betina
Kennedy, Malcolm W.
author_role author
author2 Riboldi-Tunnicliffe, Alan
Ibáñez Shimabukuro, Marina
Griffiths, Kate
Roe, Andrew J.
Cooper, Alan
Smith, Brian O.
Córsico, Betina
Kennedy, Malcolm W.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
Ascaris suum
fatty-acid-binding proteins
microfocus beamlines
parasitic nematodes
topic Bioquímica
Ascaris suum
fatty-acid-binding proteins
microfocus beamlines
parasitic nematodes
dc.description.none.fl_txt_mv 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.
Instituto de Investigaciones Bioquimicas de La Plata
description 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.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/84572
url http://sedici.unlp.edu.ar/handle/10915/84572
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1744-3091
info:eu-repo/semantics/altIdentifier/doi/10.1107/S1744309112026553
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
939-941
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.221938

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