Purification, crystallization and preliminary X-ray crystallographic analysis of rice lectin from Oryza sativa.
Lectins with sugar-binding specificity are widely distributed in higher plants and various other species. The expression of rice lectin from Oryza sativa is up-regulated in the growing coleoptile when anaerobic stress persists. A rice lectin of molecular weight 15.2 kDa has been crystallized using the hanging-drop vapour-diffusion method. From the diffraction of the lectin crystals at 1.93 A resolution, the unit cell belongs to space group P3(1), with unit-cell parameters a = 98.58, b = 98.58, c = 44.72 A. Preliminary analysis indicates that there are two lectin molecules in an asymmetric unit with a large solvent content, 70.1%.
Huang
Yen-Chieh
YC
Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.
Lin
Yi-Hung
YH
Shih
Chia-Hao
CH
Shih
Chun-Liang
CL
Chang
Tschining
T
Chen
Chun-Jung
CJ
D000693:Anaerobiosis / Q000502:physiology; D003460:Crystallization; D018360:Crystallography, X-Ray; D012275:Oryza / Q000254:growth & development / Q000378:metabolism; D018384:Oxidative Stress / Q000502:physiology; D037121:Plant Lectins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D015854:Up-Regulation
D037121:Plant Lectins; C040599:rice lectin