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  • Title: Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seeds.
    Author: Moura TR, Bezerra GA, Bezerra MJ, Teixera CS, Bezerra EH, Benevides RG, da Rocha BA, de Souza LA, Delatorre P, Nagano CS, Cavada BS.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2009 Mar 01; 65(Pt 3):213-5. PubMed ID: 19255467.
    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.
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