Crystallization and preliminary X-ray diffraction analysis of the lectin from Dioclea rostrata Benth seeds.
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.
Delatorre
Plínio
P
BioMol-Lab, Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Caixa Postal 6043, CEP 60455-970, Brazil.
Nascimento
Kyria Santiago
KS
Melo
Luciana Magalhães
LM
Souza
Emmanuel Prata de
EP
Rocha
Bruno Anderson Matias da
BA
Benevides
Raquel G
RG
Oliveira
Taiana Maia de
TM
Bezerra
Gustavo Arruda
GA
Bezerra
Maria Júlia Barbosa
MJ
Cunha
Rodrigo Maranguape Silva da
RM
Cunha
Francisco Assis Bezerra da
FA
Freire
Valder Nogueira
VN
Cavada
Benildo Sousa
BS
D003460:Crystallization; D018360:Crystallography, X-Ray; D007887:Fabaceae / Q000737:chemistry*; D037121:Plant Lectins / Q000737:chemistry* / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry*
D037121:Plant Lectins