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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):522-4. doi: 10.1107/S1744309106014795. Epub 2006 May 5.

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%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization / methods
  • Oryza / chemistry*
  • Plant Proteins / chemistry*
  • Protease Inhibitors / chemistry*
  • Solvents
  • X-Ray Diffraction

Substances

  • Plant Proteins
  • Protease Inhibitors
  • Solvents

Associated data

  • PDB/1C2A
  • PDB/1K9B
  • PDB/1PBI