Electron microscopy of two-dimensional crystals of mitochondrial ATP synthase

FEBS Lett. 1993 Dec 20;336(1):181-3. doi: 10.1016/0014-5793(93)81636-e.

Abstract

Two-dimensional crystals of the mitochondrial ATP synthase up to 0.4 microns in size were obtained from the detergent-lipid-protein micelles by detergent dialysis. A projected map of the negatively stained crystal was calculated from electron microscopical images by the Fourier-filtering procedure at about 2.8 nm resolution. The unit cell (with not more than two ATP synthase molecules) has the following parameters: a = 13.0 nm, b = 25.6 nm and gamma = 86 degrees. Two alternative models for the crystal structural organization were suggested, viz. with one or two protein molecules per unit cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Crystallization
  • Fourier Analysis
  • Microscopy, Electron
  • Mitochondria, Heart / enzymology*
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / ultrastructure

Substances

  • Proton-Translocating ATPases