Selective contrast in electron microscopy of crystalline cytochrome oxidase.
We have used various techniques for preparation of specimens for electron microscopy in order to selectively contrast different regions of vesicle crystals of cytochrome c oxidase dimers. The results are consistent with a dimer composed of two y-shaped monomers [Fuller et al., J. Mol. Biol. 134 (1979) 305] aligned along one pair of arms with the other pair of arms approximately 70 A apart. The four arms of the monomers lie within and perpendicular to the lipid bilayer in which the dimer is embedded, and the arms protrude approximately 25 A from the lipid bilayer on the matrix side of the membrane. The cytoplasmic side domains of the two monomers split away from one another forming a large cleft in the dimer. Monovalent antibodies (Fab fragments) to subunit IV appear to bind to the two monomer arms which are closely apposed across the two-fold axis of the dimer.
D003461:Crystallography / Q000379:methods*; D003576:Electron Transport Complex IV; D005614:Freeze Fracturing; D007140:Immunoglobulin Fab Fragments; D007158:Immunologic Techniques; D007425:Intracellular Membranes / Q000648:ultrastructure; D046911:Macromolecular Substances; D008563:Membrane Lipids; D008565:Membrane Proteins; D008854:Microscopy, Electron / Q000379:methods*; D008928:Mitochondria / Q000648:ultrastructure; D011487:Protein Conformation
D007140:Immunoglobulin Fab Fragments; D046911:Macromolecular Substances; D008563:Membrane Lipids; D008565:Membrane Proteins; D003576:Electron Transport Complex IV