Please use this identifier to cite or link to this item: https://repositorio.inpa.gov.br/handle/1/18792
Title: Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds
Authors: Cavada, B. S.
Marinho, Emmanuel S.
Souza, Emmanuel Prata
Benevides, R. G.
Delatorre, Plínio
Souza, Luis A.G.
Nascimento, K. S.
Sampaio, Alexandre Holanda
Moreno, Frederico Bruno Mendes Batista
Rustiguel, Joane Kathelen Rodrigues
Canduri, Fernanda
Azevedo, Walter Filgueira de
Debray, Henri
Keywords: Cymbosema Roseum
Mannose
Plant Lectin
Chromatography, Affinity
Amino Acid Sequence
Animals
Chemistry
Crystallization
Hemagglutination
Isolation And Purification
Legume
Methodology
Molecular Genetics
Seed Plant
Rabbit
X Ray Crystallography
Amino Acid Sequence
Animal
Chromatography, Affinity
Crystallization
Crystallography, X-ray
Fabaceae
Hemagglutination
Mannose
Molecular Sequence Data
Plant Lectins
Rabbits
Seeds
Issue Date: 2006
metadata.dc.publisher.journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
metadata.dc.relation.ispartof: Volume 62, Número 3, Pags. 235-237
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.
metadata.dc.identifier.doi: 10.1107/S174430910600371X
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