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

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 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.

SUBMITTER: Moura TR 

PROVIDER: S-EPMC2650465 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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

Moura Tales Rocha TR   Bezerra Gustavo Arruda GA   Bezerra Maria Julia Barbosa MJ   Teixera Cícero Silvano CS   Bezerra Eduardo Henrique Salviano EH   Benevides Raquel Guimarães RG   da Rocha Bruno Anderson Matias BA   de Souza Luiz Augusto Gomes LA   Delatorre Plínio P   Nagano Celso Shiniti CS   Cavada Benildo Sousa BS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090212 Pt 3

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 sodiu  ...[more]

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