Purification, crystallization and preliminary X-ray diffraction studies of disintegrin (schistatin) from saw-scaled viper (Echis carinatus)

Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1669-70. doi: 10.1107/s0907444901012082. Epub 2001 Oct 25.

Abstract

This is the first report of crystallographic data on a disintegrin molecule from any source. The heterodimeric disintegrin with a molecular weight of 14 kDa from Echis carinatus venom is a potent antagonist of alpha4 integrins. The intact disintegrin, containing two subunits A and B, was isolated and purified using affinity and ion-exchange columns. It has been crystallized using 1.6 M ammonium sulfate as a precipitating agent. The crystals grew to dimensions of 0.25 x 0.20 x 0.20 mm and diffracted to 2.5 A resolution. The crystals belong to space group I4(1)22, with unit-cell parameters a = b = 91.7, c = 55.1 A. Assuming a molecular weight of 14 kDa, a V(M) of 2.1 A(3) Da(-1) is obtained for one molecule of disintegrin in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Disintegrins / chemistry*
  • Protein Conformation
  • Viper Venoms / chemistry*
  • Viperidae

Substances

  • Disintegrins
  • Viper Venoms