Crystallization and preliminary X-ray diffraction analysis of the lectin from Canavalia gladiata seeds.
The seed lectin from Canavalia gladiata was purified and crystallized. Orthorhombic crystals belonging to space group C222(1) grew within three weeks at 293 K using the hanging-drop vapour-diffusion method. Using synchrotron X-ray radiation, a complete structural data set was collected at 2.3 A resolution. The preliminary crystal structure of the lectin, determined by molecular replacement, had a correlation coefficient of 0.569 and an R factor of 0.412.
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE 60451-970, Brazil.
Frederico B M B
FB
Moreno
Plínio
P
Delatorre
Beatriz T
BT
Freitas
Bruno A M
BA
Rocha
Emmanuel P
EP
Souza
Felipe
F
Facó
Fernanda
F
Canduri
André L H
AL
Cardoso
Valder N
VN
Freire
José L
JL
Lima Filho
Alexandre H
AH
Sampaio
Juan J
JJ
Calvete
Walter F
WF
De Azevedo
Benildo S
BS
Cavada
D032449:Canavalia / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D037121:Plant Lectins / Q000737:chemistry* / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry*
D037121:Plant Lectins