On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7

Detalhes bibliográficos
Autor(a) principal: Boer, D. Roeland
Data de Publicação: 2005
Outros Autores: Müller, Axel, Fetzner, Susanne, Lowe, David J., Romão, Maria João
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Texto Completo: https://doi.org/10.1107/S1744309104032105
Resumo: Isoquinoline 1-oxidoreductase (IOR) from Brevundimonas diminuta is a mononuclear molybdoenzyme of the xanthine-dehydrogenase family of proteins and catalyzes the conversion of isoquinoline to isoquinoline-1-one. Its primary sequence and behaviour, specifically in its substrate specificity and lipophilicity, differ from other members of the family. A crystal structure of the enzyme is expected to provide an explanation for these differences. This paper describes the crystallization and preliminary X-ray diffraction experiments as well as an optimized purification protocol for IOR. Crystallization of IOR was achieved using two different crystallization buffers. Streak-seeding and cross-linking were essential to obtain well diffracting crystals. Suitable cryo-conditions were found and a structure solution was obtained by molecular replacement. However, phases need to be improved in order to obtain a more interpretable electron-density map.
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spelling On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7BiophysicsStructural BiologyBiochemistryGeneticsCondensed Matter PhysicsIsoquinoline 1-oxidoreductase (IOR) from Brevundimonas diminuta is a mononuclear molybdoenzyme of the xanthine-dehydrogenase family of proteins and catalyzes the conversion of isoquinoline to isoquinoline-1-one. Its primary sequence and behaviour, specifically in its substrate specificity and lipophilicity, differ from other members of the family. A crystal structure of the enzyme is expected to provide an explanation for these differences. This paper describes the crystallization and preliminary X-ray diffraction experiments as well as an optimized purification protocol for IOR. Crystallization of IOR was achieved using two different crystallization buffers. Streak-seeding and cross-linking were essential to obtain well diffracting crystals. Suitable cryo-conditions were found and a structure solution was obtained by molecular replacement. However, phases need to be improved in order to obtain a more interpretable electron-density map.DQ - Departamento de QuímicaCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)RUNBoer, D. RoelandMüller, AxelFetzner, SusanneLowe, David J.Romão, Maria João2019-03-11T23:15:31Z2005-12-012005-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article4application/pdfhttps://doi.org/10.1107/S1744309104032105eng1744-3091PURE: 12015404http://www.scopus.com/inward/record.url?scp=33645222120&partnerID=8YFLogxKhttps://doi.org/10.1107/S1744309104032105info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-22T17:37:40Zoai:run.unl.pt:10362/63000Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T17:08:36.817277Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
title On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
spellingShingle On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
Boer, D. Roeland
Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
title_short On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
title_full On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
title_fullStr On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
title_full_unstemmed On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
title_sort On the purification and preliminary crystallographic analysis of isoquinoline 1-oxidoreductase from Brevundimonas diminuta 7
author Boer, D. Roeland
author_facet Boer, D. Roeland
Müller, Axel
Fetzner, Susanne
Lowe, David J.
Romão, Maria João
author_role author
author2 Müller, Axel
Fetzner, Susanne
Lowe, David J.
Romão, Maria João
author2_role author
author
author
author
dc.contributor.none.fl_str_mv DQ - Departamento de Química
CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)
RUN
dc.contributor.author.fl_str_mv Boer, D. Roeland
Müller, Axel
Fetzner, Susanne
Lowe, David J.
Romão, Maria João
dc.subject.por.fl_str_mv Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
topic Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
description Isoquinoline 1-oxidoreductase (IOR) from Brevundimonas diminuta is a mononuclear molybdoenzyme of the xanthine-dehydrogenase family of proteins and catalyzes the conversion of isoquinoline to isoquinoline-1-one. Its primary sequence and behaviour, specifically in its substrate specificity and lipophilicity, differ from other members of the family. A crystal structure of the enzyme is expected to provide an explanation for these differences. This paper describes the crystallization and preliminary X-ray diffraction experiments as well as an optimized purification protocol for IOR. Crystallization of IOR was achieved using two different crystallization buffers. Streak-seeding and cross-linking were essential to obtain well diffracting crystals. Suitable cryo-conditions were found and a structure solution was obtained by molecular replacement. However, phases need to be improved in order to obtain a more interpretable electron-density map.
publishDate 2005
dc.date.none.fl_str_mv 2005-12-01
2005-12-01T00:00:00Z
2019-03-11T23:15:31Z
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dc.identifier.uri.fl_str_mv https://doi.org/10.1107/S1744309104032105
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dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1744-3091
PURE: 12015404
http://www.scopus.com/inward/record.url?scp=33645222120&partnerID=8YFLogxK
https://doi.org/10.1107/S1744309104032105
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reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
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