Decamers observed in the crystals of bovine pancreatic trypsin inhibitor

Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):335-7. doi: 10.1107/S0907444998011068. Epub 1999 Jan 1.

Abstract

The structure of bovine pancreatic trypsin inhibitor (BPTI) has been solved at 2.1 A resolution in a new crystal form (space group P6422 with unit-cell dimensions a = b = 95.0, c = 158.1 A). The asymmetric unit is a pentamer, but a decamer is created by application of crystallographic symmetry. The decamer of BPTI is only the fourth such assembly reported to date in the Protein Data Bank.

Publication types

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

MeSH terms

  • Animals
  • Aprotinin / chemistry*
  • Aprotinin / isolation & purification*
  • Cattle
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Conformation

Substances

  • Aprotinin

Associated data

  • PDB/2HEX