Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa.
Bowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 A. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.
Lin
Yi-Hung
YH
Life Science Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.
Li
Hsin-Tai
HT
Huang
Yen-Chieh
YC
Hsieh
Ying-Cheng
YC
Guan
Hong-Hsiang
HH
Liu
Ming-Yih
MY
Chang
Tschining
T
Wang
Andrew H-J
AH
Chen
Chun-Jung
CJ
D003460:Crystallization / Q000379:methods; D012275:Oryza / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011480:Protease Inhibitors / Q000737:chemistry*; D012997:Solvents; D014961:X-Ray Diffraction
D010940:Plant Proteins; D011480:Protease Inhibitors; D012997:Solvents