Crystallization, data collection and phasing of black-eyed pea trypsin/chymotrypsin inhibitor in complex with bovine beta-trypsin

Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1828-30. doi: 10.1107/s090744490301641x. Epub 2003 Sep 19.

Abstract

The black-eyed pea trypsin and chymotrypsin inhibitor (BTCI) is a Bowman-Birk-type inhibitor from Vigna unguiculata seeds. A complex of BTCI with bovine beta-trypsin was crystallized by the hanging-drop vapour-diffusion method with ammonium sulfate as precipitant. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 59.3, b = 61.8, c = 80.0 A. Diffraction data were collected to 2.36 A resolution and were processed to give an overall R(sym) of 0.137. The Matthews coefficient for one complex per asymmetric unit is 2.2 A(3) Da(-1), with a corresponding solvent content of 43%. After molecular replacement and initial refinement, the model gives an R(cryst) of 0.361 and an R(free) of 0.432.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Crystallization / methods
  • Crystallography, X-Ray / methods
  • Data Collection
  • Pisum sativum / chemistry*
  • Plant Proteins / chemistry*
  • Protein Conformation
  • Seeds / chemistry
  • Trypsin / chemistry*

Substances

  • Plant Proteins
  • trypsin, chymotrypsin inhibitor, black-eyed pea
  • Trypsin