Electron microscopy of two‐dimensional crystals of mitochondrial ATP synthase

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Abstract
Two‐dimensional crystals of the mitochondrial ATP synthase up to 0.4 μm 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 γ = 86°. Two alternative models for the crystal structural organization were suggested, viz. with one or two protein molecules per unit cell.