Crystallization and preliminary X-ray crystallographic analysis of human nucleoside diphosphate kinase A

Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):503-4.

Abstract

Human nucleoside diphosphate kinase A catalyzes phosphoryl transfer and acts as a suppressor of metastasis. It has been crystallized using 2-methyl-2,4-pentanediol as a precipitant at 288 K. The crystal is monoclinic, belonging to the space group P2(1), with unit-cell parameters a = 74.21, b = 78.11, c = 82.29 A, beta = 101. 33 degrees. The asymmetric unit contains a homohexamer, with a corresponding crystal volume per protein mass (V(m)) of 2.27 A(3) Da(-1) and a solvent content of 46%. Native X-ray data to 2.15 A resolution have been collected using synchrotron X-rays.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Macromolecular Substances
  • Nucleoside-Diphosphate Kinase / chemistry*
  • Nucleoside-Diphosphate Kinase / isolation & purification
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Macromolecular Substances
  • Recombinant Proteins
  • Nucleoside-Diphosphate Kinase