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  • Title: Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa.
    Author: Lin YH, Li HT, Huang YC, Hsieh YC, Guan HH, Liu MY, Chang T, Wang AH, Chen CJ.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Jun 01; 62(Pt 6):522-4. PubMed ID: 16754971.
    Abstract:
    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%.
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