Crystallization and preliminary X-ray investigation of human erythrocytic purine nucleoside phosphorylase

J Biol Chem. 1981 Apr 25;256(8):4079-80.

Abstract

Crystals of human erythrocytic purine nucleoside phosphorylase have been grown from solutions of ammonium sulfate. The crystals are trigonal, space group R32; the hexagonal axes are a = 143.8(2) and c = 165.1(2) A. The crystals are moderately stable to x-rays and diffract beyond 3.0 A resolution. The experimental density of the crystals indicates that the molecular weight of the protein is 94,000. The three subunits are not related by crystallographic symmetry.

Publication types

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

MeSH terms

  • Crystallization
  • Erythrocytes / enzymology*
  • Humans
  • Molecular Weight
  • Pentosyltransferases / blood*
  • Protein Conformation
  • Purine-Nucleoside Phosphorylase / blood*
  • Purine-Nucleoside Phosphorylase / isolation & purification
  • X-Ray Diffraction

Substances

  • Pentosyltransferases
  • Purine-Nucleoside Phosphorylase