Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major

Detalhes bibliográficos
Autor(a) principal: Costa Tonoli, Celisa Caldana
Data de Publicação: 2009
Outros Autores: Vieira, Plinio Salmazo, Ward, Richard John, Arni, Raghuvir Krishnaswamy [UNESP], Cavalcante de Oliveira, Arthur Henrique, Murakami, Mario Tyago
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1107/S1744309109037567
http://hdl.handle.net/11449/22100
Resumo: Nucleoside diphosphate kinases (NDKs; EC 2.7.4.6) play an essential role in the synthesis of nucleotides from intermediates in the salvage pathway in all parasitic trypanosomatids and their structural studies will be instrumental in shedding light on the biochemical machinery involved in the parasite life cycle and host-parasite interactions. In this work, NDKb from Leishmania major was overexpressed in Escherichia coli, purified to homogeneity and crystallized using the sitting-drop vapour-diffusion method. The NDK crystal diffracted to 2.2 angstrom resolution and belonged to the trigonal crystal system, with unit-cell parameters a = 114.2, c = 93.9 angstrom. Translation-function calculations yielded an unambiguous solution in the enantiomorphic space group P3(2)21.
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spelling Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania majorNucleoside diphosphate kinases (NDKs; EC 2.7.4.6) play an essential role in the synthesis of nucleotides from intermediates in the salvage pathway in all parasitic trypanosomatids and their structural studies will be instrumental in shedding light on the biochemical machinery involved in the parasite life cycle and host-parasite interactions. In this work, NDKb from Leishmania major was overexpressed in Escherichia coli, purified to homogeneity and crystallized using the sitting-drop vapour-diffusion method. The NDK crystal diffracted to 2.2 angstrom resolution and belonged to the trigonal crystal system, with unit-cell parameters a = 114.2, c = 93.9 angstrom. Translation-function calculations yielded an unambiguous solution in the enantiomorphic space group P3(2)21.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Brazilian Assoc Synchrotron Light Technol, Ctr Struct Mol Biol, Campinas, SP, BrazilFFCLRP USP, Dept Chem, Ribeirao Preto, SP, BrazilIBILCE UNESP, Dept Phys, Sao Jose do Rio Preto, SP, BrazilIBILCE UNESP, Dept Phys, Sao Jose do Rio Preto, SP, BrazilFAPESP: 07/06755-2FAPESP: 07/54865CNPq: 307853/2006-3CNPq: 473997/2007-0CNPq: 471192/2007-4Wiley-Blackwell Publishing, IncBrazilian Assoc Synchrotron Light TechnolUniversidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Costa Tonoli, Celisa CaldanaVieira, Plinio SalmazoWard, Richard JohnArni, Raghuvir Krishnaswamy [UNESP]Cavalcante de Oliveira, Arthur HenriqueMurakami, Mario Tyago2014-05-20T14:02:41Z2014-05-20T14:02:41Z2009-11-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1116-1119application/pdfhttp://dx.doi.org/10.1107/S1744309109037567Acta Crystallographica Section F-structural Biology and Crystallization Communications. Malden: Wiley-blackwell Publishing, Inc, v. 65, p. 1116-1119, 2009.1744-3091http://hdl.handle.net/11449/2210010.1107/S1744309109037567WOS:000271421800010WOS000271421800010.pdf91625089789458870000-0003-2460-1145Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengActa Crystallographica Section F: Structural Biology and Crystallization Communicationsinfo:eu-repo/semantics/openAccess2023-10-06T06:01:17Zoai:repositorio.unesp.br:11449/22100Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T14:07:44.125440Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
title Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
spellingShingle Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
Costa Tonoli, Celisa Caldana
title_short Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
title_full Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
title_fullStr Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
title_full_unstemmed Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
title_sort Production, purification, crystallization and preliminary X-ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
author Costa Tonoli, Celisa Caldana
author_facet Costa Tonoli, Celisa Caldana
Vieira, Plinio Salmazo
Ward, Richard John
Arni, Raghuvir Krishnaswamy [UNESP]
Cavalcante de Oliveira, Arthur Henrique
Murakami, Mario Tyago
author_role author
author2 Vieira, Plinio Salmazo
Ward, Richard John
Arni, Raghuvir Krishnaswamy [UNESP]
Cavalcante de Oliveira, Arthur Henrique
Murakami, Mario Tyago
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Brazilian Assoc Synchrotron Light Technol
Universidade de São Paulo (USP)
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Costa Tonoli, Celisa Caldana
Vieira, Plinio Salmazo
Ward, Richard John
Arni, Raghuvir Krishnaswamy [UNESP]
Cavalcante de Oliveira, Arthur Henrique
Murakami, Mario Tyago
description Nucleoside diphosphate kinases (NDKs; EC 2.7.4.6) play an essential role in the synthesis of nucleotides from intermediates in the salvage pathway in all parasitic trypanosomatids and their structural studies will be instrumental in shedding light on the biochemical machinery involved in the parasite life cycle and host-parasite interactions. In this work, NDKb from Leishmania major was overexpressed in Escherichia coli, purified to homogeneity and crystallized using the sitting-drop vapour-diffusion method. The NDK crystal diffracted to 2.2 angstrom resolution and belonged to the trigonal crystal system, with unit-cell parameters a = 114.2, c = 93.9 angstrom. Translation-function calculations yielded an unambiguous solution in the enantiomorphic space group P3(2)21.
publishDate 2009
dc.date.none.fl_str_mv 2009-11-01
2014-05-20T14:02:41Z
2014-05-20T14:02:41Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1107/S1744309109037567
Acta Crystallographica Section F-structural Biology and Crystallization Communications. Malden: Wiley-blackwell Publishing, Inc, v. 65, p. 1116-1119, 2009.
1744-3091
http://hdl.handle.net/11449/22100
10.1107/S1744309109037567
WOS:000271421800010
WOS000271421800010.pdf
9162508978945887
0000-0003-2460-1145
url http://dx.doi.org/10.1107/S1744309109037567
http://hdl.handle.net/11449/22100
identifier_str_mv Acta Crystallographica Section F-structural Biology and Crystallization Communications. Malden: Wiley-blackwell Publishing, Inc, v. 65, p. 1116-1119, 2009.
1744-3091
10.1107/S1744309109037567
WOS:000271421800010
WOS000271421800010.pdf
9162508978945887
0000-0003-2460-1145
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Acta Crystallographica Section F: Structural Biology and Crystallization Communications
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1116-1119
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 Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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