Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds
dc.contributor.author | Cavada, B. S. | |
dc.contributor.author | Marinho, Emmanuel S. | |
dc.contributor.author | Souza, Emmanuel Prata | |
dc.contributor.author | Benevides, R. G. | |
dc.contributor.author | Delatorre, Plínio | |
dc.contributor.author | Souza, Luis A.G. | |
dc.contributor.author | Nascimento, K. S. | |
dc.contributor.author | Sampaio, Alexandre Holanda | |
dc.contributor.author | Moreno, Frederico Bruno Mendes Batista | |
dc.contributor.author | Rustiguel, Joane Kathelen Rodrigues | |
dc.contributor.author | Canduri, Fernanda | |
dc.contributor.author | Azevedo, Walter Filgueira de | |
dc.contributor.author | Debray, Henri | |
dc.date.accessioned | 2020-06-15T22:03:04Z | |
dc.date.available | 2020-06-15T22:03:04Z | |
dc.date.issued | 2006 | |
dc.description.abstract | A lectin from Cymbosema roseum seeds (CRL) was purified, characterized and crystallized. The best crystals grew in a month and were obtained by the vapour-diffusion method using a precipitant solution consisting of 0.1 M Tris-HCl pH 7.8, 8%(w/v) PEG 3350 and 0.2 M proline at a constant temperature of 293 K. A data set was collected to 1.77 Å resolution at a synchrotron-radiation source. CRL crystals are orthorhombic, belonging to space group P212121. Crystallographic refinement and full amino-acid sequence determination are in progress. © 2006 International Union of Crystallography. All rights reserved. | en |
dc.identifier.doi | 10.1107/S174430910600371X | |
dc.identifier.uri | https://repositorio.inpa.gov.br/handle/1/18792 | |
dc.language.iso | en | pt_BR |
dc.publisher.journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | pt_BR |
dc.relation.ispartof | Volume 62, Número 3, Pags. 235-237 | pt_BR |
dc.rights | Restrito | * |
dc.subject | Cymbosema Roseum | en |
dc.subject | Mannose | en |
dc.subject | Plant Lectin | en |
dc.subject | Chromatography, Affinity | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | Animals | en |
dc.subject | Chemistry | en |
dc.subject | Crystallization | en |
dc.subject | Hemagglutination | en |
dc.subject | Isolation And Purification | en |
dc.subject | Legume | en |
dc.subject | Methodology | en |
dc.subject | Molecular Genetics | en |
dc.subject | Seed Plant | en |
dc.subject | Rabbit | en |
dc.subject | X Ray Crystallography | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | Animal | en |
dc.subject | Chromatography, Affinity | en |
dc.subject | Crystallization | en |
dc.subject | Crystallography, X-ray | en |
dc.subject | Fabaceae | en |
dc.subject | Hemagglutination | en |
dc.subject | Mannose | en |
dc.subject | Molecular Sequence Data | en |
dc.subject | Plant Lectins | en |
dc.subject | Rabbits | en |
dc.subject | Seeds | en |
dc.title | Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds | en |
dc.type | Artigo | pt_BR |