Selective contrast in electron microscopy of crystalline cytochrome oxidase

T. G. Frey, M. J. Costello, S. H.P. Chan

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

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 Å 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 Å 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.

Original languageEnglish (US)
Pages (from-to)85-91
Number of pages7
JournalUltramicroscopy
Volume13
Issue number1-2
DOIs
StatePublished - 1984

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Atomic and Molecular Physics, and Optics
  • Instrumentation

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