Mitochondrial ATP synthase. Quaternary structure of the F1 moiety at 3.6 A determined by x-ray diffraction analysis.
Open Access
- 1 November 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (31) , 21197-21201
- https://doi.org/10.1016/s0021-9258(18)54840-7
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Molecular architecture of Escherichia coli F1 adenosinetriphosphataseBiochemistry, 1989
- The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301Journal of Molecular Biology, 1987
- Molecular-replacement structure of guinea pig IgGl pFc' refined at 3.1Å resolutionActa crystallographica Section B, Structural science, crystal engineering and materials, 1985
- Electron microscopy of beef heart mitochondrial F1‐ATPaseFEBS Letters, 1984
- Use of monoclonal antibodies in immuno-electron microscopy for the determination of subunit stoichiometry in oligomeric enzymes: There are three α-subunits in the F1-ATPase of Escherichia coliJournal of Molecular Biology, 1984
- An Electron Microscopic Approach to the Quaternary Structure of Mitochondrial F1‐ATPaseEuropean Journal of Biochemistry, 1983
- The oscillation method for crystals with very large unit cellsActa Crystallographica Section A, 1979
- Structure of ATPase (coupling factor TF1) from a thermophilic bacteriumJournal of Molecular Biology, 1977
- Adenosine triphosphatase from rat liver mitochondria — Evidence for a mercurial-sensitive site for the activating anion bicarbonateBiochemical and Biophysical Research Communications, 1976
- The treatment of errors in the isomorphous replacement methodActa Crystallographica, 1959