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Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seeds. 2009
Tales Rocha Moura, and
Gustavo Arruda Bezerra, and
Maria Julia Barbosa Bezerra, and
Cícero Silvano Teixera, and
Eduardo Henrique Salviano Bezerra, and
Raquel Guimarães Benevides, and
Bruno Anderson Matias da Rocha, and
Luiz Augusto Gomes de Souza, and
Plínio Delatorre, and
Celso Shiniti Nagano, and
Benildo Sousa Cavada
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
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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