Crystallization and preliminary X-ray studies of purine nucleoside phosphorylase from Cellulomonas sp

Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1061-3. doi: 10.1107/s0907444998004120.

Abstract

The commercially available enzyme purine nucleoside phosphorylase (PNP) from Cellulomonas sp. was purified by ion--exchange chromatography, partially sequenced and crystallized in two different crystal forms using the hanging-drop vapour-diffusion technique. Crystal form A grows as polyeders and/or cubes in the cubic space group P4232 with unit-cell dimension a = 162.5 A. Crystal form B appears as thick plates in the space group P212121 with unit-cell dimensions a = 63.2, b = 108.3 and c = 117.4 A. Both crystal forms contain three monomers (one trimer) in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Gram-Positive Asporogenous Rods / enzymology*
  • Protein Conformation*
  • Purine-Nucleoside Phosphorylase / chemistry*
  • Purine-Nucleoside Phosphorylase / isolation & purification
  • Sequence Analysis

Substances

  • Bacterial Proteins
  • Purine-Nucleoside Phosphorylase