Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa

被引:0
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作者
Lin, Yi-Hung
Li, Hsin-Tai
Huang, Yen-Chieh
Hsieh, Ying-Cheng
Guan, Hong-Hsiang
Liu, Ming-Yih
Chang, Tschining
Wang, Andrew H. -J. [1 ]
Chen, Chun-Jung
机构
[1] Natl Synchrotron Radiat Res Ctr, Life Sci Grp, Div Res, Hsinchu 30076, Taiwan
[2] Natl Tsing Hua Univ, Inst Bioinformat & Struct Biol, Hsinchu 30013, Taiwan
[3] Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan
[4] Natl Tsing Hua Univ, Dept Phys, Hsinchu 30013, Taiwan
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷
关键词
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中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom, 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 angstrom. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.
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页码:522 / 524
页数:3
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