Crystallization and preliminary X-ray analysis of recombinant histone HPhA from the hyperthermophilic archaeon Pyrococcus horikoshii OT3

Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):870-1. doi: 10.1107/s0907444902005036. Epub 2002 Apr 26.

Abstract

Recombinant archaeal histone from the hyperthermophile Pyrococcus horikoshii OT3 (HPhA) was crystallized by the hanging-drop vapour-diffusion method. Crystals grew at 291 K in 200 mM (NH(4))(2)SO(4), 100 mM sodium acetate buffer pH 4.6, 19% PEG 4000. Diffraction data were obtained to a resolution of 2.3 A from a single frozen crystal, which belonged to space group P2(1) with unit-cell parameters a = 34.99, b = 46.89, c = 35.02 A, alpha = gamma = 90, beta = 104 degrees. The asymmetric unit contained two molecules and had a solvent content of approximately 35%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Escherichia coli / genetics
  • Histones / chemistry*
  • Histones / genetics
  • Protein Conformation
  • Pyrococcus / chemistry*
  • Pyrococcus / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • X-Ray Diffraction

Substances

  • Histones
  • Recombinant Proteins