| Literature DB >> 16511292 |
Plínio Delatorre1, Kyria Santiago Nascimento, Luciana Magalhães Melo, Emmanuel Prata de Souza, Bruno Anderson Matias da Rocha, Raquel G Benevides, Taiana Maia de Oliveira, Gustavo Arruda Bezerra, Maria Júlia Barbosa Bezerra, Rodrigo Maranguape Silva da Cunha, Francisco Assis Bezerra da Cunha, Valder Nogueira Freire, Benildo Sousa Cavada.
Abstract
Lectins from the Diocleinae subtribe (Leguminosae) are highly similar proteins that promote various biological activities with distinctly differing potencies. The structural basis for this experimental data is not yet fully understood. Dioclea rostrata lectin was purified and crystallized by hanging-drop vapour diffusion at 293 K. The crystal belongs to the orthorhombic space group I222, with unit-cell parameters a = 61.51, b = 88.22, c = 87.76 A. Assuming the presence of one monomer per asymmetric unit, the solvent content was estimated to be about 47.9%. A complete data set was collected at 1.87 A resolution.Entities:
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Year: 2006 PMID： 16511292 PMCID： PMC2150952 DOI： 10.1107/S1744309106001801
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091