| Literature DB >> 19255467 |
Tales Rocha Moura1, Gustavo Arruda Bezerra, Maria Julia Barbosa Bezerra, Cícero Silvano Teixera, Eduardo Henrique Salviano Bezerra, Raquel Guimarães Benevides, Bruno Anderson Matias da Rocha, Luiz Augusto Gomes de Souza, Plínio Delatorre, Celso Shiniti Nagano, Benildo Sousa Cavada.
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.Entities:
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Year: 2009 PMID: 19255467 PMCID: PMC2650465 DOI: 10.1107/S1744309109000797
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091