• Publications
  • Influence
The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules.
  • R. Henderson
  • Physics
    Quarterly reviews of biophysics
  • 1 May 1995
TLDR
Because of the lack of sufficiently bright neutron sources in the foreseeable future, electron microscopy in practice provides the greatest potential for immediate progress.
Electron-crystallographic refinement of the structure of bacteriorhodopsin.
TLDR
Using electron diffraction data corrected for diffuse scattering together with additional phase information from 30 new images of tilted specimens, an improved experimental density map has been calculated for bacteriorhodopsin and the overall accuracy of the co-ordinates of residues in the other six helices has been improved.
MRC image processing programs.
TLDR
This paper describes the current state of a large set of programs written by various members of the Laboratory of Molecular Biology for processing images of two-dimensional crystals and of particles with helical or icosahedral symmetry for determination of macromolecular structures by electron microscopy.
Three-dimensional model of purple membrane obtained by electron microscopy
TLDR
A 7-Å resolution map of the purple membrane has been obtained by electron microscopy of tilted, unstained specimens and shows that Lipid bilayer regions fill the spaces between the protein molecules.
Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction
  • R. Henderson
  • Physics
    Proceedings of the Royal Society of London…
  • 23 July 1990
By using the fading of electron diffraction patterns during electron irradiation of protein or other organic crystals as a benchmark to measure destruction of the crystalline atomic arrangement by
Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
TLDR
An atomic model for structural changes involved in the vectorial, light-driven transport of protons by bacteriorhodopsin is presented, which provides an ‘opening’ of the protein to protons on the cytoplasmic side of the membrane.
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