Electron microscopy of beef heart mitochondrial F1‐ATPase

@article{Tsuprun1984ElectronMO,
  title={Electron microscopy of beef heart mitochondrial F1‐ATPase},
  author={V. Tsuprun and I. V. Mesyanzhinova and I. Kozlov and E. Orlova},
  journal={FEBS Letters},
  year={1984},
  volume={167}
}
The quaternary structure of isolated and membrane‐bound F1‐ATPase (submitochondrial particles) has been studied by electron microscopy. A model of the molecule has been proposed: six protein masses are arranged in two layers approximately at the vertices of a triangular antiprism. Computer averaging of the images showed that the frontal view of the molecule can be approximately characterized by mirror plane symmetry. 
Structure of the ATP‐synthase studied by electron microscopy and image processing
The structure of ATP synthase from beef heart mitochondria has been studied by electron microscopy and image processing using negatively stained specimens of detergent‐solubilized and membrane‐boundExpand
Electron microscopy of two‐dimensional crystals of mitochondrial ATP synthase
TLDR
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 by the Fourier‐filtering procedure and two alternative models for the crystal structural organization were suggested. Expand
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  • Biology, Medicine
  • Microscopy research and technique
  • 1994
TLDR
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Structure of mitochondrial F1-ATPase studied by electron microscopy and image processing.
TLDR
The structure of soluble F1-ATPase (EC 3.1.3) has been investigated by computer analysis of individual molecular images extracted from electron micrographs of negatively stained particles and possible subunit arrangements and their consequences for the mechanism of ATP synthesis are discussed. Expand
Electron microscopy of the reconstituted complexes of the F1‐ATPase with various subunit constitution revealed the location of the γ subunit in the central cavity of the molecule
TLDR
It is concluded that the central mass in the F1‐ATPase is comprised mostly of the γ subunit, similar to that found in the native enzyme (α3β3γδϵ). Expand
Electron microscopy and image analysis of the complexes I and V of the mitochondrial respiratory chain.
TLDR
It can be taken as proven that the energy transmitted to the ATP synthase is used to induce a conformational change in the latter enzyme, in such a way as to bring about the energy-requiring dissociation of already synthesized ATP. Expand
Structure of the ATP synthase from chloroplasts studied by electron microscopy. Localization of the small subunits
TLDR
The structure of the hydrophilic part of the ATP synthase from chloroplasts (CF1) has been further investigated by electron microscopy and image analysis of negatively stained samples andsequences for the mechanism of ATP synthesis are discussed. Expand
On the Structure of the ATP-Synthase from Chloroplasts
TLDR
The H+-translocating ATPase from chloroplasts is a membrane-bound enzyme which can couple a transmembrane proton transport with ATP synthesis/hydrolysis and there is no general agreement about the subunit stoichiometry up to now. Expand
Molecular architecture of Escherichia coli F1 adenosinetriphosphatase.
TLDR
The structure of the E. coli F1 ATPase (ECF1) has been studied by a novel combination of two specimen preparation and image analysis techniques, yielding a more informative description of the enzyme than otherwise possible. Expand
Structure of the ATP-synthase from chloroplasts studied by electron microscopy and image processing.
TLDR
The structure of the hydrophilic part of the ATP synthase from chloroplasts (CF1) has been investigated by electron microscopy of negatively stained samples and shows that all projections are of a hexagonal or flattened hexagonal type. Expand
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Electron microscopy of beef heart F1-ATPase crystals.
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Abstract 1. 1. A subunit (ETPH) having nearly theoretical P/O ratios may be prepared from heavy mitochondria from beef heart when both Mg2+ and Mn2+ are included in the medium during the isolationExpand
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