Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri
| Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
|---|---|
| Data(s) |
18/04/2012
18/04/2012
2009
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| Resumo |
Maltose-binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 Kusing the hanging-drop vapour-diffusion method. The crystal belonged to the primitive hexagonal space group P6(1)22, with unit-cell parameters a = 123.59, b = 123.59, c = 304.20 angstrom, and contained two molecules in the asymetric unit. It diffracted to 2.24 angstrom resolution. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)[01/07540-3] Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)[04/02716-4] Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)[00/10266-8] Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) Associacao Brasileira de Tecnologia de Luz Sincrotron (ABTLuS) US Department of Energy (DOE) |
| Identificador |
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.65, p.105-107, 2009 1744-3091 http://producao.usp.br/handle/BDPI/15868 10.1107/S1744309108041833 |
| Idioma(s) |
eng |
| Publicador |
WILEY-BLACKWELL PUBLISHING, INC |
| Relação |
Acta Crystallographica Section F-structural Biology and Crystallization Communications |
| Direitos |
closedAccess Copyright WILEY-BLACKWELL PUBLISHING, INC |
| Palavras-Chave | #ESCHERICHIA-COLI #CRYSTAL-STRUCTURE #ACTIVE-TRANSPORT #LIGAND-BINDING #2 MODES #CHEMOTAXIS #RECEPTOR #Biochemical Research Methods #Biochemistry & Molecular Biology #Biophysics #Crystallography |
| Tipo |
article original article publishedVersion |
