Crystallization and preliminary X-ray analysis of inorganic pyrophosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3

Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):577-9. doi: 10.1107/S0907444904000630. Epub 2004 Feb 25.

Abstract

Inorganic pyrophosphatase (PPase; EC 3.6.1.1) from the hyperthermophile Pyrococcus horikoshii was crystallized by the hanging-drop vapour-diffusion method at pH 5.0 using polyethyleneglycol 4000 as the precipitant. The crystal belongs to space group P2(1)2(1)2, with unit-cell parameters a = 71.7, b = 86.5, c = 92.5 A, alpha = beta = gamma = 90 degrees. There are two molecules in the asymmetric unit. The crystals were stable during exposure to X-rays and a full set of X-ray diffraction data was collected to 2.7 A resolution in-house.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Hydrogen-Ion Concentration
  • Inorganic Pyrophosphatase / chemistry*
  • Polyethylene Glycols
  • Pyrococcus horikoshii / enzymology*
  • Recombinant Proteins / chemistry

Substances

  • Recombinant Proteins
  • Polyethylene Glycols
  • Inorganic Pyrophosphatase