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Título: | Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seeds |
Autor: | Moura, Tales R. Bezerra, Gustavo Arruda Bezerra, Maria Marques Teixera, Cícero Silvano Bezerra, Eduardo Henrique Salviano Benevides, R. G. Rocha, Bruno Anderson Matias da Souza, Luis Augusto Gomes de Delatorre, Plínio Nagano, C. S. Cavada, B. S. |
Palavras-chave: | Lectin, Canavalia Plant Lectin Chromatography, Affinity Canavalia Chemistry Crystallization Seed Plant Electrophoresis, Polyacrylamide Gel X Ray Crystallography Canavalia Chromatography, Affinity Crystallization Crystallography, X-ray Electrophoresis, Polyacrylamide Gel Plant Lectins Seeds Canavalia Canavalia Boliviana Fabaceae Piperaceae |
Data do documento: | 2009 |
Revista: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
É parte de: | Volume 65, Número 3, Pags. 213-215 |
Abstract: | Plant lectins are the most studied group of carbohydrate-binding proteins. Despite the high similarity between the members of the Diocleinae subtribe (Leguminosae) group, they present differing biological activities. Canavalia boliviana lectin (Cbol) was purified using a Sephadex G-50 column and crystallized in the presence of X-Man by hanging-drop vapour diffusion at 293 K. After optimization, crystals suitable for diffraction were obtained under the condition 0.1 M HEPES pH 7.5 and 3.0 M sodium formate. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 126.70, b = 66.64, c = 64.99 Å, α = 90.0, β = 120.8, γ = 90.0°. Assuming the presence of a dimer in the asymmetric unit, the solvent content was estimated to be about 46%. A complete data set was collected at 1.5 Å resolution. © 2009 International Union of Crystallography All rights reserved. |
DOI: | 10.1107/S1744309109000797 |
Aparece nas coleções: | Artigos |
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