Richard A. Henderson

Research interests

Publications

• Comparison of optimal performance at 300keV of three direct electron detectors for use in low dose electron microscopy

  Ultramicroscopy · 2014 · https://doi.org/10.1016/j.ultramic.2014.08.002

• High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy

  Ultramicroscopy · 2013 · https://doi.org/10.1016/j.ultramic.2013.06.004

• Outcome of the First Electron Microscopy Validation Task Force Meeting

  Structure · 2012 · https://doi.org/10.1016/j.str.2011.12.014

• Beam-induced motion of vitrified specimen on holey carbon film

  Journal of Structural Biology · 2012 · https://doi.org/10.1016/j.jsb.2012.02.003

• Structure of a β1-adrenergic G-protein-coupled receptor

  Nature · 2008 · https://doi.org/10.1038/nature07101

• Optimal Determination of Particle Orientation, Absolute Hand, and Contrast Loss in Single-particle Electron Cryomicroscopy

  Journal of Molecular Biology · 2003 · https://doi.org/10.1016/j.jmb.2003.07.013

• Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

  Nature · 2000 · https://doi.org/10.1038/35020614

• Protein conformational changes in the bacteriorhodopsin photocycle 1 1Edited by B. Honig

  Journal of Molecular Biology · 1999 · https://doi.org/10.1006/jmbi.1999.2589

• Electron-crystallographic Refinement of the Structure of Bacteriorhodopsin

  Journal of Molecular Biology · 1996 · https://doi.org/10.1006/jmbi.1996.0328

• MRC Image Processing Programs

  Journal of Structural Biology · 1996 · https://doi.org/10.1006/jsbi.1996.0003

• The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules

  Quarterly Reviews of Biophysics · 1995 · https://doi.org/10.1017/s003358350000305x

• Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

  The EMBO Journal · 1993 · https://doi.org/10.1002/j.1460-2075.1993.tb05625.x

• Projection structure of rhodopsin

  Nature · 1993 · https://doi.org/10.1038/362770a0

• Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

  Journal of Molecular Biology · 1990 · https://doi.org/10.1016/s0022-2836(05)80271-2

• Structure of purple membrane from halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution

  Ultramicroscopy · 1986 · https://doi.org/10.1016/0304-3991(86)90203-2

• Three-dimensional structure determination by electron microscopy of two-dimensional crystals

  Progress in Biophysics and Molecular Biology · 1982 · https://doi.org/10.1016/0079-6107(83)90017-2

• Path of the polypeptide in bacteriorhodopsin.

  Proceedings of the National Academy of Sciences · 1980 · https://doi.org/10.1073/pnas.77.4.2023

• Three-dimensional model of purple membrane obtained by electron microscopy

  Nature · 1975 · https://doi.org/10.1038/257028a0

• The structure of the purple membrane from Halobacterium halobium: Analysis of the X-ray diffraction pattern

  Journal of Molecular Biology · 1975 · https://doi.org/10.1016/0022-2836(75)90123-0

• Molecular structure determination by electron microscopy of unstained crystalline specimens

  Journal of Molecular Biology · 1975 · https://doi.org/10.1016/0022-2836(75)90212-0

• Structure of crystalline α-chymotrypsin

  Journal of Molecular Biology · 1968 · https://doi.org/10.1016/s0022-2836(68)80043-9

• Three-dimensional Structure of Tosyl-α-chymotrypsin

  Nature · 1967 · https://doi.org/10.1038/214652a0

Current projects

No projects listed.