Formation, crystallization, and preliminary crystallographic data of the ternary complex of alpha-chymotrypsin, beta-trypsin, and the Bowman-Birk inhibitor

J Biol Chem. 1981 Nov 25;256(22):11417-9.

Abstract

The ternary complex of the Bowman-Birk inhibitor with alpha-chymotrypsin and beta-trypsin has been crystallized and preliminary crystallographic information describing the crystals has been obtained. The crystals are triclinic with unit cell dimensions: a = 51.96 A, b = 56.34 A, c = 46.70 A, alpha = 98.83 degrees, beta = 97.29 degrees, and gamma = 97.15 degrees. There is 1 ternary complex/unit cell and the diffraction pattern extends to 2.2 A resolution. The search for heavy atom derivatives based on known derivatives of chymotrypsin and trypsin is underway.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chymotrypsin*
  • Crystallization
  • Protein Binding
  • Protein Conformation
  • Trypsin Inhibitor, Bowman-Birk Soybean*
  • Trypsin Inhibitors*
  • Trypsin*
  • X-Ray Diffraction

Substances

  • Trypsin Inhibitor, Bowman-Birk Soybean
  • Trypsin Inhibitors
  • Chymotrypsin
  • Trypsin