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.
Moreno
Frederico B M B
FB
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE 60451-970, Brazil.
Delatorre
Plínio
P
Freitas
Beatriz T
BT
Rocha
Bruno A M
BA
Souza
Emmanuel P
EP
Facó
Felipe
F
Canduri
Fernanda
F
Cardoso
André L H
AL
Freire
Valder N
VN
Lima Filho
José L
JL
Sampaio
Alexandre H
AH
Calvete
Juan J
JJ
De Azevedo
Walter F
WF
Cavada
Benildo S
BS
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