Adenosine triphosphatase from rat liver mitochondria. Crystallization and x-ray diffraction studies of the F1-component of the enzyme

J Biol Chem. 1978 Apr 10;253(7):2067-9.


The homogeneous rat liver F1-ATPase preparation of Catterall and Pedersen (Catterall, W.A., and Pedersen, P.L. (1971) J. Biol. Chem. 246, 4987-4994) has been crystallized from a solution containing phosphate and ATP by precipitation with ammonium sulfate. Most of the resultant crystals are cubes of approximately 0.3 to 0.6 mm per side. X-ray precession photographs show that the crystals are rhombohedral, space group R32 (D37 NO155) with hexagonal cell dimensions a = 148 A, c = 368 A. The molecular weight of the asymmetric unit of the crystals is 190,000 or about half the molecular weight (384,000) of the rat liver enzyme indicating that the crystallographic 2-fold axes of symmetry coincide with a molecular symmetry axis. The crystals diffract to at least 3.5 A and therefore this is the first report of an ATPase preparation in which crystals suitable for x-ray analysis have been obtained.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases* / isolation & purification
  • Animals
  • Crystallization
  • Isoenzymes / isolation & purification
  • Macromolecular Substances
  • Mitochondria, Liver / enzymology*
  • Protein Conformation
  • Rats
  • X-Ray Diffraction


  • Isoenzymes
  • Macromolecular Substances
  • Adenosine Triphosphatases