Preliminary crystallographic data for Bowman-Birk inhibitor from soybean seeds.
A well characterized soybean protease inhibitor, the Bowman-Birk inhibitor, has been crystallized at room temperature in the presence of polyethylene glycol 4000 by vapor diffusion against an ammonium sulfate solution containing 2-methyl-2,4-pentanediol. An x-ray diffraction study reveals that the inhibitor crystallizes in a hexagonal unit cell of symmetry P6122 (or P6522) and dimensions a = b = 91.36(2) A and c = 63.92(2) A. Each of the 12 asymmetric units contains 2 molecules of molecular weight 8000. The crystal, which diffracts barely to 3-A spacings, is fairly stable to x-irradiation and has a solvent content of approximately 52% by volume.
D003460:Crystallization; D011487:Protein Conformation; D012639:Seeds; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D014361:Trypsin Inhibitors; D014961:X-Ray Diffraction
D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D014361:Trypsin Inhibitors