Neutron macromolecular crystallography with LADI-III

Autores
Blakeley, Matthew P.; Teixeira, Susana C. M.; Petit Haertlein, Isabelle; Hazemann, Isabelle; Mitschler, Andre; Haertlein, Michael; Howard, Eduardo Ignacio; Podjarny, Alberto D.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
At the Institut Laue-Langevin, a new neutron Laue diffractometer LADI-III has been fully operational since March 2007. LADI-III is dedicated to neutron macromolecular crystallography at medium to high resolution (2.5-1.5 Å) and is used to study key H atoms and water structure in macromolecular structures. An improved detector design and readout system has been incorporated so that a miniaturized reading head located inside the drum scans the image plate. From comparisons of neutron detection efficiency (DQE) with the original LADI-I instrument, the internal transfer of the image plates and readout system provides an approximately threefold gain in neutron detection. The improved performance of LADI-III, coupled with the use of perdeuterated biological samples, now allows the study of biological systems with crystal volumes of 0.1-0.2 mm3, as illustrated here by the recent studies of type III antifreeze protein (AFP; 7 kDa). As the major bottleneck for neutron macromolecular studies has been the large crystal volumes required, these recent developments have led to an expansion of the field, extending the size and the complexity of the systems that can be studied and reducing the data-collection times required.
Fil: Blakeley, Matthew P.. No especifíca;
Fil: Teixeira, Susana C. M.. No especifíca;
Fil: Petit Haertlein, Isabelle. No especifíca;
Fil: Hazemann, Isabelle. Inserm; Francia
Fil: Mitschler, Andre. Inserm; Francia
Fil: Haertlein, Michael. No especifíca;
Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Podjarny, Alberto D.. Inserm; Francia
Materia
ANTIFREEZE PROTEIN
NEUTRON MACROMOLECULAR CRYSTALLOGRAPHY
LADI-III
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/277254

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Neutron macromolecular crystallography with LADI-IIIBlakeley, Matthew P.Teixeira, Susana C. M.Petit Haertlein, IsabelleHazemann, IsabelleMitschler, AndreHaertlein, MichaelHoward, Eduardo IgnacioPodjarny, Alberto D.ANTIFREEZE PROTEINNEUTRON MACROMOLECULAR CRYSTALLOGRAPHYLADI-IIIhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1At the Institut Laue-Langevin, a new neutron Laue diffractometer LADI-III has been fully operational since March 2007. LADI-III is dedicated to neutron macromolecular crystallography at medium to high resolution (2.5-1.5 Å) and is used to study key H atoms and water structure in macromolecular structures. An improved detector design and readout system has been incorporated so that a miniaturized reading head located inside the drum scans the image plate. From comparisons of neutron detection efficiency (DQE) with the original LADI-I instrument, the internal transfer of the image plates and readout system provides an approximately threefold gain in neutron detection. The improved performance of LADI-III, coupled with the use of perdeuterated biological samples, now allows the study of biological systems with crystal volumes of 0.1-0.2 mm3, as illustrated here by the recent studies of type III antifreeze protein (AFP; 7 kDa). As the major bottleneck for neutron macromolecular studies has been the large crystal volumes required, these recent developments have led to an expansion of the field, extending the size and the complexity of the systems that can be studied and reducing the data-collection times required.Fil: Blakeley, Matthew P.. No especifíca;Fil: Teixeira, Susana C. M.. No especifíca;Fil: Petit Haertlein, Isabelle. No especifíca;Fil: Hazemann, Isabelle. Inserm; FranciaFil: Mitschler, Andre. Inserm; FranciaFil: Haertlein, Michael. No especifíca;Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Podjarny, Alberto D.. Inserm; FranciaWiley Blackwell Publishing, Inc2010-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/277254Blakeley, Matthew P.; Teixeira, Susana C. M.; Petit Haertlein, Isabelle; Hazemann, Isabelle; Mitschler, Andre; et al.; Neutron macromolecular crystallography with LADI-III; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 66; 11; 10-2010; 1198-12050907-4449CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.iucr.org/paper?S0907444910019797info:eu-repo/semantics/altIdentifier/doi/10.1107/S0907444910019797info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T14:44:35Zoai:ri.conicet.gov.ar:11336/277254instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-12-23 14:44:36.184CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Neutron macromolecular crystallography with LADI-III
title Neutron macromolecular crystallography with LADI-III
spellingShingle Neutron macromolecular crystallography with LADI-III
Blakeley, Matthew P.
ANTIFREEZE PROTEIN
NEUTRON MACROMOLECULAR CRYSTALLOGRAPHY
LADI-III
title_short Neutron macromolecular crystallography with LADI-III
title_full Neutron macromolecular crystallography with LADI-III
title_fullStr Neutron macromolecular crystallography with LADI-III
title_full_unstemmed Neutron macromolecular crystallography with LADI-III
title_sort Neutron macromolecular crystallography with LADI-III
dc.creator.none.fl_str_mv Blakeley, Matthew P.
Teixeira, Susana C. M.
Petit Haertlein, Isabelle
Hazemann, Isabelle
Mitschler, Andre
Haertlein, Michael
Howard, Eduardo Ignacio
Podjarny, Alberto D.
author Blakeley, Matthew P.
author_facet Blakeley, Matthew P.
Teixeira, Susana C. M.
Petit Haertlein, Isabelle
Hazemann, Isabelle
Mitschler, Andre
Haertlein, Michael
Howard, Eduardo Ignacio
Podjarny, Alberto D.
author_role author
author2 Teixeira, Susana C. M.
Petit Haertlein, Isabelle
Hazemann, Isabelle
Mitschler, Andre
Haertlein, Michael
Howard, Eduardo Ignacio
Podjarny, Alberto D.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ANTIFREEZE PROTEIN
NEUTRON MACROMOLECULAR CRYSTALLOGRAPHY
LADI-III
topic ANTIFREEZE PROTEIN
NEUTRON MACROMOLECULAR CRYSTALLOGRAPHY
LADI-III
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv At the Institut Laue-Langevin, a new neutron Laue diffractometer LADI-III has been fully operational since March 2007. LADI-III is dedicated to neutron macromolecular crystallography at medium to high resolution (2.5-1.5 Å) and is used to study key H atoms and water structure in macromolecular structures. An improved detector design and readout system has been incorporated so that a miniaturized reading head located inside the drum scans the image plate. From comparisons of neutron detection efficiency (DQE) with the original LADI-I instrument, the internal transfer of the image plates and readout system provides an approximately threefold gain in neutron detection. The improved performance of LADI-III, coupled with the use of perdeuterated biological samples, now allows the study of biological systems with crystal volumes of 0.1-0.2 mm3, as illustrated here by the recent studies of type III antifreeze protein (AFP; 7 kDa). As the major bottleneck for neutron macromolecular studies has been the large crystal volumes required, these recent developments have led to an expansion of the field, extending the size and the complexity of the systems that can be studied and reducing the data-collection times required.
Fil: Blakeley, Matthew P.. No especifíca;
Fil: Teixeira, Susana C. M.. No especifíca;
Fil: Petit Haertlein, Isabelle. No especifíca;
Fil: Hazemann, Isabelle. Inserm; Francia
Fil: Mitschler, Andre. Inserm; Francia
Fil: Haertlein, Michael. No especifíca;
Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Podjarny, Alberto D.. Inserm; Francia
description At the Institut Laue-Langevin, a new neutron Laue diffractometer LADI-III has been fully operational since March 2007. LADI-III is dedicated to neutron macromolecular crystallography at medium to high resolution (2.5-1.5 Å) and is used to study key H atoms and water structure in macromolecular structures. An improved detector design and readout system has been incorporated so that a miniaturized reading head located inside the drum scans the image plate. From comparisons of neutron detection efficiency (DQE) with the original LADI-I instrument, the internal transfer of the image plates and readout system provides an approximately threefold gain in neutron detection. The improved performance of LADI-III, coupled with the use of perdeuterated biological samples, now allows the study of biological systems with crystal volumes of 0.1-0.2 mm3, as illustrated here by the recent studies of type III antifreeze protein (AFP; 7 kDa). As the major bottleneck for neutron macromolecular studies has been the large crystal volumes required, these recent developments have led to an expansion of the field, extending the size and the complexity of the systems that can be studied and reducing the data-collection times required.
publishDate 2010
dc.date.none.fl_str_mv 2010-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/277254
Blakeley, Matthew P.; Teixeira, Susana C. M.; Petit Haertlein, Isabelle; Hazemann, Isabelle; Mitschler, Andre; et al.; Neutron macromolecular crystallography with LADI-III; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 66; 11; 10-2010; 1198-1205
0907-4449
CONICET Digital
CONICET
url http://hdl.handle.net/11336/277254
identifier_str_mv Blakeley, Matthew P.; Teixeira, Susana C. M.; Petit Haertlein, Isabelle; Hazemann, Isabelle; Mitschler, Andre; et al.; Neutron macromolecular crystallography with LADI-III; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 66; 11; 10-2010; 1198-1205
0907-4449
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://journals.iucr.org/paper?S0907444910019797
info:eu-repo/semantics/altIdentifier/doi/10.1107/S0907444910019797
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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