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

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

Yi-Hung Lin, Hsin-Tai Li, Yen-Chieh Huang, Ying-Cheng Hsieh, Hong-Hsiang Guan, Ming-Yih Liu, Tschining Chang, Andrew H.-J. Wang and Chun-Jung Chen
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol.62(6), pp.522-524
06/2006

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 Å. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%. © 2006 International Union of Crystallography. All rights reserved.

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