Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia boliviana Piper seeds.
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.
Moura
Tales Rocha
TR
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brazil.
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
D032449:Canavalia / Q000737:chemistry*; D002846:Chromatography, Affinity; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D037121:Plant Lectins / Q000032:analysis / Q000737:chemistry*; D012639:Seeds / Q000737:chemistry*
D037121:Plant Lectins; C039268:lectin, Canavalia