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 cry...
| Autor principal: | Moura, Tales R. |
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| Outros Autores: | Bezerra, Gustavo Arruda, Bezerra, Maria Marques, Teixera, Cícero Silvano, Bezerra, Eduardo Henrique Salviano, Benevides, R. G., Rocha, Bruno Anderson Matias da, Souza, Luis Augusto Gomes de, Delatorre, Plínio, Nagano, C. S., Cavada, B. S. |
| Grau: | Artigo |
| Idioma: | English |
| Publicado em: |
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
2020
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| Acesso em linha: |
https://repositorio.inpa.gov.br/handle/1/18454 |
| Resumo: |
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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 Å, α = 90.0, β = 120.8, γ = 90.0°. 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 Å resolution. © 2009 International Union of Crystallography All rights reserved. |