Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seeds.

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作者:Moura Tales Rocha, Bezerra Gustavo Arruda, Bezerra Maria Julia Barbosa, Teixera Cícero Silvano, Bezerra Eduardo Henrique Salviano, Benevides Raquel Guimarães, da Rocha Bruno Anderson Matias, de Souza Luiz Augusto Gomes, Delatorre Plínio, Nagano Celso Shiniti, Cavada Benildo Sousa
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 A, alpha = 90.0, beta = 120.8, gamma = 90.0 degrees . 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 A resolution.

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