Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase

This publication has 19 references indexed in Scilit:

• THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE
  Annual Review of Biochemistry, 1997
• Direct observation of the rotation of F1-ATPase
  Nature, 1997
• Solution structure of the N-terminal domain of the δ subunit of the E. coli ATPsynthase
  Nature Structural & Molecular Biology, 1997
• Topographical structure of membrane‐bound Escherichia coli F₁F₀ ATP synthase in aqueous buffer
  FEBS Letters, 1996
• Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
  Nature Structural & Molecular Biology, 1995
• The F₀ Complex of the Escherichia Coli ATP Synthase
  European Journal of Biochemistry, 1995
• Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
  Nature, 1994
• Coupling between catalytic sites and the proton channel in F1F0-type ATPases
  Trends in Biochemical Sciences, 1994
• Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy
  Biochemistry, 1990
• The stalk connecting the F₁ and F₀ domains of ATP synthase visualized by electron microscopy of unstained specimens
  FEBS Letters, 1987