Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of rice Bowman–Birk inhibitor from Oryza sativa
Author(s) -
Lin YiHung,
Li HsinTai,
Huang YenChieh,
Hsieh YingCheng,
Guan HongHsiang,
Liu MingYih,
Chang Tschining,
Wang Andrew H.J.,
Chen ChunJung
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106014795
Subject(s) - oryza sativa , crystallization , proteases , germination , crystallography , x ray crystallography , chemistry , broken rice , solvent , resolution (logic) , botany , biology , stereochemistry , biochemistry , enzyme , diffraction , organic chemistry , gene , physics , artificial intelligence , computer science , optics , raw material , bran
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 Å, the unit cell belongs to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 74.37, b = 96.69, c = 100.36 Å. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%.