Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor

J Mol Biol. 1992 Oct 5;227(3):942-4. doi: 10.1016/0022-2836(92)90234-b.


Cathepsin B from bovine spleen has been purified and crystallized as a complex with a specific inhibitor CA074 [N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L- isoleucyl-L-proline], using the hanging-drop method. The complex crystals obtained from 50 mM-citrate buffer (pH 3.5) belong to the tetragonal space group P4(1) (or P4(3)) with a = 73.06 A and c = 141.59 A, and diffract beyond 2.2 A resolution. There are two complex molecules per asymmetric unit giving a packing density of 3.37 A3/Da and indicating a high solvent content of 63.5%.

MeSH terms

  • Animals
  • Cathepsin B / chemistry*
  • Cathepsin B / metabolism
  • Cattle
  • Crystallization
  • Dipeptides / chemistry*
  • Dipeptides / metabolism
  • Macromolecular Substances
  • Models, Chemical
  • X-Ray Diffraction


  • Dipeptides
  • Macromolecular Substances
  • N-(3-propylcarbamoyloxirane-2-carbonyl)-isoleucyl-proline
  • Cathepsin B