Russo, C.J. & Henderson, R.
Ultramicroscopy. 187, 26-33 (2018)
Ewald sphere correction using a single side-band image processing algorithm.

Russo, C.J. & Henderson, R. 
Ultramicroscopy. 187, 56-63 (2018)
Microscopic charge fluctuations cause minimal contrast loss in cryoEM.

Russo, C.J. & Henderson, R. 
Ultramicroscopy. 187, 43-49 (2018)
Charge accumulation in electron cryomicroscopy.

Henderson, R.
J. Struct. Biol. 200, 202-203 (2017)
An adventure with Don.

Tkach, K.
BioCenturyInnovations 14July2016, 12-15 (2016)
Cryo-EM: A River.

Henderson, R. 
Times Higher Education 2259, 22-23 (16-22 June issue, 2016).
HE&Me.

McMullan, G, Faruqi, A.R. & Henderson, R.
Methods in Enzymology 579, 1-17 (2016).
Direct Electron Detectors.

Vinothkumar, K.R. & Henderson, R. 
Quart. Rev. Biophysics 49, e13, 1-25 (2016).
Single particle electron cryomicroscopy: trends, issues and future perspective.

Subramaniam, S., Kuhlbrandt, W. & Henderson, R.
IUCrJ 3, 3-7 (2016).
CryoEM at IUCrJ: a new era.

Faruqi, A.R., Henderson, R. & McMullan, G.
Advances in Imaging and Electron Optics 190, 103-141 (2015).
Chapter Two – Progress and Development of direct Detectors for Electron Cryomicroscopy.

Sali, A., Berman, H.M., Schwede, T., Trewhella, J., Kleywegt, G., Burley, S.K., Markley, J., Nakamura, H., Adams, P., Bonvin, A.M.J.J., Chiu, Dal Peraro, M., Di Maio, F., W., Ferrin, T.E., Grünewald, K., Gutmanas, A., Henderson, R., Hummer, G., Iwasaki, K., Johnson, G., Lawson, C.L., Meiler, J., Marti-Renom, M.A., Montelione, G.T., Nilges, M., Nussinov, R., Patwardhan, A., Rappsilber, J., Read, R.J., Saibil, H., Schröder, G.F., Schwieters, C.D., Seidel, C.A.M., Svergun, D., Topf, M., Ulrich, E.L., Velankar, S. & Westbrook, J.D.
Structure 23, 1-12 (2015).
Outcome of the First wwPDB Hybrid / Integrative Methods Task Force Workshop.

Cheng, A., Henderson, R., Mastronarde, D., Ludtke, S.J., Schoenmakers, R.H.M., Short, J., Marabini, R., Dallakyan, S., Agard, D. & Winn, M. 
J. Struct. Biol. 192, 146-150 (2015).
MRC2014: Extensions to the MRC format header for electron cryo-microscopy and tomography.

Henderson, R. 
Archives of Biochemistry and Biophysics, 581, 19-24 (2015).
Overview and future of single particle electron cryomicroscopy.

Slowik, D. & Henderson, R.
Biochem. Biophys. Acta 1848, 1545-1551 (2015).
Benchmarking the stability of human detergent-solubilised voltage-gated sodium channels for structural studies using eel as a reference.

McMullan, G., Vinothkumar, K.R. & Henderson, R.
Ultramicroscopy 158, 26-32 (2015).
Thon rings from amorphous ice and implications for beam-induced Brownian motion in single particle electron cryo-microscopy.

McMullan, G., Faruqi, A.R., Clare, D. & Henderson, R. 
Ultramicroscopy 147, 156-163 (2014).
Comparison of optimal performance at 300 keV of three direct electron detectors for use in low dose electron microscopy.

Faruqi, A.R., Henderson, R. & McMullan, G.
Proceedings of Science, PoS(Vertex 2013)044, (11 pages). In proceedings of “22nd International Workshop on Vertex Detectors” (Vertex 2013), September 15-20, 2013, Lake Starnberg, Germany.
Recent Developments in Direct Electron Detectors for Electron Cryo-Microscopy.

Vinothkumar, K.R., McMullan, G. & Henderson, R.  
Structure 22, 621-627 (2014).
Molecular mechanism of antibody-mediated activation of β-galactosidase.

Henderson, R. 
Nature 504, 93-94 (2013).
News & Views: Ion channel seen by electron microscopy.

Henderson, R. 
Proc. Nat. Acad. Sci. USA 110, 18037-18041 (2013).
Avoiding the pitfalls of single particle cryoEM: Einstein from noise.

Chen, S., McMullan, G., Faruqi, A.R., Murshudov, G.N., Short, J.M., Scheres, S.H. & Henderson, R.
Ultramicroscopy 135, 24-35 (2013).
High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy.

Henderson, R. & McMullan, G.
Microscopy (Tokyo) 62, 43-50 (2013).
Problems in obtaining perfect images by single particle electron cryomicroscopy of biological structures in amorphous ice.

Patwardhan, A., Carazo, J.-M., Carragher, B., Henderson, R., Heymann, J.B., Hill, E., Jensen, G.J., Lagerstedt, I., Lawson, C.L., Ludtke, S.J., Mastronarde, D., Moore, W.J., Roseman, A., Rosenthal, P., Sorzano, C.-O.S., Sanz-García, E., Scheres, S.H.W., Subramaniam, S., Westbrook, J., Winn, M., Swedlow, J.R. & Kleywegt, G.J.
Nature Structural and Molecular Biology 19, 1203-1207 (2012).
Data management challenges in three-dimensional EM.

Brilot, A.F., Chen, J.Z., Cheng, A.,  Pan, J., Harrison, S.C., Potter, C.S., Carragher, B., Henderson, R. & Grigorieff, N.
J. Struct. Biol. 177, 630-637 (2012)  [doi: 10.1016/j.jsb.2012.02.003].
Beam-induced motion of vitrified specimen on holey carbon film.

Henderson, R., Sali, A., Berman, H.M., Chiu, W., Kleywegt, G.J., Lawson, C.L., Baker, M.L., Carragher, B., Devkota, B., Downing, K.H., Egelman, E.H., Feng, Z., Frank, J, Grigorieff, N., Jiang, W., Ludtke, S.J., Medalia, O., Penczek, P.A., Rosenthal, P.B., Rossmann, M.G., Schmid, M.F., Schröder, G.F., Steven, A.C., Stokes, D.L., Westbrook, J.D., Wriggers, W., Yang, H. & Young, J.
Structure 20, 205-214 (2012)   [doi: 10.1016/j.str.2011.12.014].
Outcome of the first electron microscopy validation task force meeting.

Baker, T.S. & Henderson, R. (published 27 January 2012)
In:  International Tables for Crystallography, Vol. F (second edition), "Crystallography of Biological Macromolecules",  (Ed. Rossmann, M.G. & Arnold, E.).  Wiley. 
Electron cryomicroscopy of biological macromolecules.

Henderson, R., Chen, S., Chen, J.Z., Grigorieff, N., Passmore, L.A., Ciccarelli, L., Rubinstein, J.L., Crowther, R.A., Stewart, P.L. & Rosenthal. P.B. 
J. Mol. Biol. 413, 1028-1046 (2011)    [doi:10.1016/j.jmb.2011.09.008].
Tilt-pair analysis of images from a range of different specimens in single particle electron cryomicroscopy.

Guerrini, N.,Turchetta, R., Van Hoften, G., Henderson, R., McMullan, G. & Faruqi, A.R.
J. Inst. 6, C03003 (2011)   [doi:10.1088/1748-0221/6/03/C03003].
A high frame rate, 16 million pixels, radiation hard CMOS sensor.

Glaeser, R.M., McMullan, G., Henderson, R. & Faruqi, A.R. 
Ultramicroscopy 111, 90-100 (2011).
Images of paraffin monolayer crystals with perfect contrast: Minimization of beam-induced specimen motion.

Vinothkumar, K.R.
J. Mol. Biol. 407, 232-247 (2011).
Structure of rhomboid protease in a lipid environment.

Vinothkumar, K.R., Strisovsky, K., Andreeva, A., Christova, Y., Verhelst, S. & Freeman, M. 
EMBO J. 29, 3797-3809 (2010).
The structural basis for catalysis and substrate specificity of a rhomboid protease.

Vinothkumar, K.R. & Henderson, R. 
Quarterly Reviews of Biophysics, 43, 65-158 (2010).
Structures of Membrane Proteins.

Henderson, R. & Franks, N.P.
In Biogr. Mems Fell. R. Soc. 55, 13-35 (2009).
David Mervyn Blow : 27 June 1931 - 8 June 2004.

McMullan, G., Turchetta, R., Clarke, A. & Faruqi, A.R.
Ultramicroscopy 109, 1411-1416 (2009).
Enhanced Imaging in Low Dose Electron Microscopy Using Electron Counting.

McMullan, G., Faruqi, A.R. Henderson, R., Guerrini, N., Turchetta, R., Jacobs, A & van Hoften, G.  
Ultramicroscopy 109, 1144-1147 (2009).
Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector.

McMullan, G., Chen, S., Henderson, R. & Faruqi, A.R. 
Ultramicroscopy 109, 1126-1143 (2009).
Detective quantum efficiency of electron area detectors.

Warne, T., Serrano-Vega, M.J., Baker, J.G., Moukhametzianov, R., Edwards, P.C., Henderson, R., Leslie, A.G.W., Tate, C.G. & Schertler, G.F.X. 
Nature 454, 486-491 (2008).
Structure of a β1-adrenergic G-protein-coupled receptor.

Faruqi, A.R. & Henderson, R. 
Current Opinion in Structural Biology 17, 549-555 (2007).
Electronic detectors for electron microscopy.

McMullan, G., Cattermole, D.M., Chen, S., Henderson, R., Llopart, X., Summerfield, C., Tlustos, L. & Faruqi, A.R.
Ultramicroscopy 107, 401-413 (2007).
Electron imaging with Medipix2 hybrid pixel detector.

Henderson, R., Cattermole, D., McMullan, G., Scotcher, S., Fordham, M., Amos, W.B. & Faruqi, A.R.   
Ultramicroscopy 107, 73-80 (2007).
Digitisation of electron microscope films: six useful tests applied to three film scanners

Faruqi, A.R., Henderson, R. & Holmes, J.
Nucl. Instr. & Meth. in Phys. Res. A565, 139-143 (2006).
Radiation damage studies on STAR250 CMOS sensor at 300 keV for electron microscopy.

Turchetta, R., Allport, P.P., Casse, G., Clark, A., Crooks, J., Evans, A., Fant, A., Faruqi, A.R., French, M.J., Henderson, R., Morrissey, Q., Prior, D., Prydderch, M., Velthius, J.J., Villani, G., Waltham, N., Willmore, B. & Willmore, P. 
Nucl. Instr. & Meth. in Phys. Res. A560, 139-142 (2006).
CMOS monolithic active pixel sensors (MAPS): New ‘eyes’ for science.

Evans, D.A., Allport, P.P., Casse, G., Faruqi, A.R., Gallop, B., Henderson, R., Prydderch, M., Turchetta, A.R., Tyndel, M., Velthius, J., Villani, G. & Waltham, N. 
Nucl. Instr. & Meth. in Phys. Res. A546, 281-285 (2005).
CMOS active pixel sensors for ionizing radiation.

Faruqi, A.R., Henderson, R. Prydderch, M., Allport, P. & Evans, A.
Nucl. Instr. & Meth. in Phys. Res. A546, 170-175 (2005).
Direct single electron detection with a CMOS detector or for electron microscopy.

Faruqi,  A.R., Henderson, R. & Tlustos, L. 
Nucl. Instr. & Meth. in Phys. Res. A546, 160-163 ( 2005).
Noiseless direct detection of electrons in Medipix 2 for electron microscopy.

Henderson, R. 
Nature Structural & Molecular Biology 11, 680- 681 ( 2004).
David Blow, 1931- 2004.

Henderson, R.
The Independent (UK national newspaper) 23 June, 2004, Obituary pages.
Professor David Blow:  Pioneer of protein crystallography at Cambridge, and Imperial College, London.

Henderson, R
Quart. Rev. Biophys. 37, 3-13 (2004).
Realizing the potential of electron cryo-microscopy.

Rubinstein, J.L., Walker, J.E. & Henderson, R. 
EMBO J. 22, 6182-6192 (2003).
Structure of the mitochondrial ATP synthase by electron cryomicroscopy.

Rosenthal, P.B. & Henderson, R.
J. Mol. Biol. 333, 721-742 (2003).
Optimal determination of particle orientation, absolute hand, and contrast loss in single particle electron cryomicroscopy. 
With an Appendix:  Rosenthal, P.B., Crowther, R.A. & Henderson, R. 
J. Mol. Biol. 333, 743-745 (2003).
An objective criterion for resolution assessment in single-particle electron microscopy.

Henderson, R.
In:  Excellence in Science; April 2003, Royal Society Newsletter, p.10.
Half-time in a century of molecular biology.

Faruqi, A.R., Cattermole, D.M., Henderson, R., Mikulec, B. & Raeburn, C.
Ultramicroscopy 94, 263-276 (2003).
Evaluation of a hybrid pixel detector for electron microscopy.

Henderson, R. 
Nature 415, 833-833 (2002).
Excitement over X-ray lasers is excessive – Structural biology is a rich field in which existing techniques are providing many advances.

Subramaniam, S. Hirai, T. & Henderson, R.
Phil. Trans. Roy. Soc. A. 360, 859-874 (2002).
From structure to mechanism:  electron crystallographic studies of bacteriorhodopsin.

Rhee, K.-H., Scarborough, G.A. & Henderson, R.
EMBO J. 21, 3582-3589 (2002).
Domain movements of plasma membrane H+-ATPase:  3D structures of two states by electron cryo-miocroscopy.

Henderson, R.
Structure 10, 455-458 (2002).
Max Perutz (1914-2002):  Great Scientist and Modest Leader.

Henderson, R.
Cell 109, 13-16 (2002).
Max Perutz (1914-2002):  Great Scientist and Modest Leader.

Tittor, J., Paula, S., Subramaniam, S., Heberle, J., Henderson, R. & Oesterhelt, D. 
J. Mol. Biol. 319, 555-565 (2002).
Proton translocation by bacteriorhodopsin in the absence of substantial conformational changes.

Milne, J.S., Shi, D., Rosenthal, P.B., Sunshine, J.S., Domingo, G.J., Wu, X., Brooks, B.R., Perham, R.N., Henderson, R. & Subramaniam, S.
EMBO J. 21, 5587-5598 (2002).
Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex:  a multifunctional catalytic machine.

Baker, T.S. & Henderson, R. (2001),
In:  International Tables for Crystallography, Vol. F, "Crystallography of Biological Macromolecules",  Chapter 19.6 pp. 451-463;  473-479.  (Ed. Rossmann, M.G. & Arnold, E.).  Dordrecht: Kluwer Academic Publishers.
Electron cryomicroscopy.

Kunji, E.R.S., Spudich, E.N., Grisshammer, R., Henderson, R. & Spudich, J.L.
J. Mol. Biol. 308, 279-293 (2001).
Electron crystallographic analysis of two-dimensional crystals of sensory rhodopsin II:  A 6.9Å projection structure.

Henderson, R.
Nature Struct. Biol. 7, 271-272 (2000).
Paul Sigler:  A structural biologist with passion (obituary).

Subramaniam, S. & Henderson, R. 
Biochimica et Biophysica Acta - Bioenergetics, 1460, 157-165 (2000).
Crystallographic analysis of protein conformational changes in the bacteriorhodopsin photocycle.

Subramaniam, S. & Henderson, R. 
Nature 406, 653-657 (2000).
Molecular mechanism for vectorial proton translocation by bacteriorhodopsin.

Kunji, E.R.S., von Gronau, S. Oesterhelt, D. & Henderson, R.
Proc. Nat. Acad. Sci. USA 97, 4637-4642 (2000).
Three-dimensional structure of halorhodopsin to 5Å by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure.

Subramaniam, S. & Henderson, R.
J. Struct. Biol. 128, 19-25 (1999).
Electron crystallography of bacteriorhodopsin with millisecond time resolution.

Faruqi, A.R., Henderson, R. & Subramaniam, S.
Ultramicroscopy 75, 235-250 (1999).
Cooled CCD detector with tapered fibre optics for recording electron diffraction patterns.

Bullough, P.A. & Henderson, R.
J. Mol. Biol. 286, 1663-1771 (1999).
Projection structure of the K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction.

Subramaniam, S., Lindahl, M., Bullough, P.A., Faruqi, W., Tittor, J., Oesterhelt, D. Brown, L., Lanyi, J. & Henderson, R.
J. Mol. Biol. 287, 145-161 (1999).
Protein conformational changes in the bacteriorhodopsin photocycle.

Grigorieff, N.
J. Mol. Biol. 277, 1033-1046 (1998).
Three-dimensional structure of bovine NADH:Ubiquinone Oxidoreductase (Complex I) at 22Å in ice.

Henderson, R.
Novartis Foundation Symposium 213, 36-55 (1998).
on "The Limits of Reductionism in Biology".  Ed. Jamie Goode.
Macromolecular structure and self-assembly.

Henderson, R.
In:  "The Electron:  Proceedings of the International Centennial Symposium on the Electron"  p.183-197 (1998).
Edited by A. Kirkland & P.D. Brown, published by the Institute of Materials Communications Ltd.
Atomic resolution 3D-structures of biological molecules by electron microscopy.

Lindahl, M. & Henderson, R.
Ultramicroscopy, 70, 95-106 (1997).
Structure of the bacteriorhodopsin D85N/D96N double mutant showing substantial structural changes and a highly twinned, disordered lattice.

Subramaniam, S., Faruqi, A.R., Oesterhelt, D. & Henderson, R.
Proc. Natl. Acad. Sci. USA 94, 1767-1772 (1997).
Electron diffraction studies of light-induced conformational changes in the Leu-93->Ala bacteriorhodopsin mutant.

Henderson R. & Unwin, N. 
In:  "Time-resolved diffraction", p.391-400 (1997).  OUP, edited by J.R. Helliwell & P.M. Rentzepis:
Time-resolved electron diffraction and microscopy studies of membrane proteins.

Henderson, R.
Structure 4, 1115-1116 (1996).
The coming of age of biological electron microscopy.  
Book Review of "Three-dimensional electron microscopy of macromolecular assemblies"  by Joachim Frank, Academic Press, 1996.

Grigorieff, N. & Henderson, R.
Ultramicroscopy 65, 101-107 (1996).
Comparison of calculated and observed dynamical diffraction from purple membrane:  implications.

Grigorieff, N., Ceska, T.A., Downing, K.H., Baldwin, J.M. & Henderson, R.
J. Mol. Biol. 259, 393-421 (1996).
Electron-crystallographic refinement of the structure of bacteriorhodopsin.

Crowther, R.A., Henderson, R. & Smith, J.M.
J. Struct. Biol. 116, 9-16 (1996)
MRC image processing programs.

Faruqi, A.R., Andrews, H.N. & Henderson, R.
Nucl. Instr. & Meth. Phys. Res. A367, 408-412 (1995).
A high sensitivity imaging detector for electron microscopy.

Grigorieff, N., Beckmann, E. & Zemlin, F.
J. Mol. Biol. 254, 404-415 (1995).
Lipid location in Deoxycholate-treated purple membrane at 2.6Å.

Moffat, J.K. & Henderson, R.
Curr. Opin. Struct. Biol. 5, 656-663 (1995).
Freeze trapping of reaction intermediates.

Grigorieff, N. & Henderson, R.
Ultramicroscopy 60, 295-309 (1995).
Diffuse scattering in electron diffraction data from protein crystals.

Henderson, R. &  Faruqi, A.R.
Ultramicroscopy 60, 375-383 (1995).
Analysis of sensitivity of cold stages on Philips CM12 to sources of vibration.

Henderson R. 
Quart. Rev. Biophysics 28, 171-193 (1995).
The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules.

Karrasch, S. Bullough, P.A. & Ghosh, R.
EMBO J. 14, 631-638 (1995)
The 8.5Å projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits.

Havelka, W.A., Henderson, R. & Oesterhelt, D.
J. Mol. Biol. 247, 726-738 (1995).
Three-dimensional structure of halorhodopsin at 7Å resolution.

Valpuesta, J.M., Carrascosa, J.L. & Henderson, R.   
J. Mol. Biol. 240, 281-287 (1994).
Analysis of electron microscope images and electron diffraction patterns of thin crystals of Ø29 connectors in ice.

Biesecker, G., Lachmann, P. & Henderson, R.
Molecular Immunology 30, 1369-1382 (1993).
Structure of complement poly-C9 determined in projection by cryo-electron microscopy and single particle analysis.

Frank, J., Chiu, W. & Henderson, R.
Ultramicroscopy 49, 387-396 (1993).
Flopping polypeptide chains and Suleika's subtle imperfections:  analysis of variations in the electron micrograph of a purple membrane crystal.

Grisshammer, R., Duckworth, R. & Henderson, R.
Biochemical Journal 295, 571-576 (1993).
Expression of a rat neurotensin receptor in Escherichia coli.

Havelka, W.A., Henderson, R., Heymann, J.A.W. & Oesterhelt, D.
J. Mol. Biol. 234, 837-846 (1993).
Projection structure of Halorhodopsin at 6.1Å obtained by electron cryo-microscopy.

Schertler, G.F.X., Villa, C. & Henderson, R.
Nature 362, 770-772 (1993).
Projection structure of rhodopsin.

Henderson, R.
In:  Les Cahiers de la Fondation Louis Jeantet, 8, 39-50 (1993).
Electron microscopic analysis of the structure of bacteriorhodopsin.

Baldwin, J.M., Beckmann, E., Ceska, T.A., Downing, K.H., Henderson, R. & Zemlin, F.   
Structure 0, xx (1993).
Bacteriorhodopsin.

Subramaniam, S., Gerstein, M., Oesterhelt, D. & Henderson, R. 
EMBO J. 12, 1-8 (1993).
Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

Rigler, R. & Henderson, R.
Quart. Rev. Biophysics 25, 379-380 (1992)
Peter Lauger (1934-1990)

Ceska, T.A., Henderson, R., Baldwin, J.M., Zemlin, F., Beckmann, E. & Downing, K.
Acta Physiol. Scand. 146, 31-40 (1992).
An atomic model for the structure of bacteriorhodopsin, a seven-helix membrane protein.

Henderson, R.   
Ultramicroscopy 46, 1-18 (1992).
Image contrast in high resolution electron microscopy of biological macromolecules:  TMV in ice.

Henderson, R. & Baldwin, J.M.   
MRC News 50, 20-21 (1991).
Bacteriorhodopsin and seven-helix membrane receptor proteins.

Cattermole, D. & Henderson, R.
Ultramicroscopy 35, 55-57 (1991).
An electronic image drift compensator for electron microscopy.

Henderson, R., Raeburn, C.S. & Vigers, G.
Ultramicroscopy 35, 45-53 (1991).
A side-entry cold holder for cryo-electron microscopy.

Bullough, P.A. & Tulloch, P.A.
Ultramicroscopy 35, 131-143 (1991).
Spot-scan imaging of an influenza neuraminidase-antibody fragment complex.

Bullough, P.A. & Tulloch, P.A.
J. Mol. Biol. 215, 161-173 (1990).
High resolution spot-scan electron microscopy of microcrystals of an α-helical coiled-coil protein.

Bullough, P.A. & Henderson, R.
Biophysical J. 58, 705-711 (1990).
Phase accuracy in high-resolution electron microscopy of trigonal and orthorhombic purple membrane.

Henderson, R.
Proc. Roy. Soc. B241, 6-8 (1990).
Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction.

Ceska, T.A. & Henderson, R.
J. Mol. Biol. 213, 539-560 (1990).
Analysis of high resolution electron diffraction patterns from purple membrane labelled with heavy atoms.

Caspar, D.L.D.
Nature, News & Views 345, 666-667 (1990).
Bacteriorhodopsin - at last!

Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E. & Downing, K.H.
Biochem. Soc. Transact. 18, 844 (1990).
An atomic model for the structure of bacteriorhodopsin.

Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E. & Downing, K.H.
J. Mol. Biol. 213, 899-929 (1990).
A model for the structure of bacteriorhodopsin based on high resolution electron cryo-microscopy.

Valpuesta, J.M., Henderson, R. & Frey, T.G.
J. Mol. Biol. 214, 237-251 (1990).
An electron cryo-microscopic analysis of crystalline cytochrome oxidase.

Henderson, R. & Schertler, G.
Phil. Trans. Roy. Soc. B326, 379-389 (1990).
The structure of bacteriorhodopsin, and its relevance to the visual opsins and other seven helix G-protein receptors.

Pande, C. Callender, R., Henderson, R. & Pande, A.
Biochemistry, 28, 5971-5978 (1989).
Purple membrane - color, crystallinity and the effect of DMSO.

Baldwin, J.M., Henderson, R., Beckmann, E. & Zemlin, F.
J. Mol. Biol. 202, 585-591 (1988).
Images of purple membranes at 2.8 Å resolution obtained by cryo-electron microscopy.

Li, J., Henderson, R., Carroll, J. & Ellar, D.
J. Mol. Biol. 199, 543-544 (1988).
X-ray analysis of the crystalline parasporal inclusion in Bacillus thuringiensis var. tenebrionis.

Bullough, P. & Henderson, R.
Ultramicroscopy 21, 223-230 (1987).
Use of spot-scan procedure for recording low-dose micrographs of beam sensitive specimens.

Henderson, R., Baldwin, J.M., Ceska, T.A, Glaeser, R.M. & Tsygannik, I.N.
In "Retinal Proteins", VNU Science Press, Netherlands, p. 153-171 (1987).  Ed. Y.A.  Ovchinnikov.  Proceedings of Lake Baikal Conference on Retinal Proteins, USSR. July 1986.
Structure analysis of bacteriorhodopsin by electron crystallography.

Tsygannik, I.N. & Baldwin, J.M.
Eur. Biophys. J., 14, 263-272 (1987).
Three dimensional structure of deoxycholate-treated purple membranes at 6 Å resolution and molecular averaging of three crystal forms of bacteriorhodopsin.

Baldwin, J.M. Ceska, T.A., Glaeser, R.M. & Henderson, R.
Proc. of meeting "Crystallography in Molecular Biology", Bischenberg, Sept. 85, Plenum Pub. New York, (Eds.) Moras, D., Drenth, J., Standberg, B., Suck, D. & Wilson, K. NATO Asi Series A, Vol. 126, pp. 101-115 (1987).
Structure analysis of bacteriorhodopsin by electron crystallography.

Henderson, R. & Baldwin, J.M.
In "44th Annual Proc. of EMSA" (Ed.) G.W. Bailey, 6-9 (1986).
Treatment of gradient of defocus in images of tilted, thin crystals.

Henderson, R., Baldwin, J.M., Downing, K., Lepault, J. & Zemlin, F
Ultramicroscopy 19, 147-178 (1986).
Structure of purple membrane from Halobacterium halobium:  recording, measurement and evaluation of electron micrographs at 3.5 Å resolution.

Glaeser, R.M., Baldwin, J.M., Ceska, T.A. & Henderson, R.
Biophysical J. 50, 913-920 (1986).
Electron diffraction analysis of the M412 intermediate of bacteriorhodopsin.

Henderson, R.
Nature, News and Views 318, 598-599 (1985).
Structure of a bacterial photosynthetic reaction centre.

Glaeser, R.M., Jubb, J.S. & Henderson, R.
Biophysical J. 48, 775-780 (1985).
Structural comparison of native and deoxycholate-treated purple membrane.

Henderson, R. & Glaeser, R.M.
Ultramicroscopy 16, 139-150 (1985).
Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals.

Jubb, J.S., Worcester, D.L., Crespi, H.L. & Zaccai, G.
EMBO J., 3, 1455-1461 (1984).
Retinal location in purple membrane of Halobacterium halobium:  a neutron diffraction study of membranes labelled in vivo with deuterated retinal.

Baldwin, J.M. & Henderson, R.
Ultramicroscopy 14, 319-336 (1984).
Measurement and evaluation of electron diffraction patterns from two-dimensional crystals.

Amos, L.A., Jubb, J.S., Henderson, R. & Vigers, G.
J. Mol. Biol. 178, 711-729 (1984).
Arrangement of protofilaments in two forms of tubulin crystal induced by vinblastine.

Unwin, P.N.T. & Henderson, R.
Scientific American 250, (2), 78-94 (1984).
The structure of proteins in biological membranes.

Henderson, R., Baldwin, J.M., Agard, D.A. & Leifer, D.
In "41st Annual Proc. Electron Microscopy Soc. Amer." (Ed.) G.W. Bailey p. 418-421 (1983).
High resolution structural analysis of purple membrane.

Leifer, D. & Henderson, R.
J. Mol. Biol. 163, 451-466 (1983).
Three-dimensional structure of orthorhombic purple membrane at 6.5 Å resolution.

Wallace, B.A. & Henderson, R.
Biophys. J. 39, 233-239 (1982).
Location of the carboxyl terminus of bacteriorhodospin in purple membrane.

Fuller, S.D., Capaldi, R.A. & Henderson, R.
Biochemistry, 21, 2525-2529 (1982).
Preparation of two-dimensional arrays from purified beef heart cytochrome c oxidase.

Deatherage, J.F., Henderson, R. & Capaldi, R.A.
J. Mol. Biol. 158, 501-514 (1982).
Relationship between membrane and cytoplasmic domains in cytochrome c oxidase by electron microscopy in media of different density.

Deatherage, J.F., Henderson, R. & Capaldi, R.A.
J. Mol. Biol. 158, 487-499 (1982).
Three-dimensional structure of cytochrome c oxidase vesicle crystals in negative stain.

Amos, L.A., Henderson, R. & Unwin, P.N.T.
Prog. Biophys. & Mol. Biol. 39, 183-231 (1982).
Three-dimensional structure determination by electron microscopy of two-dimensional crystals.

Rossmann, M.G. & Henderson, R.
Acta Cryst. A38, 13-20 (1982).
Phasing electron diffraction amplitudes with the molecular replacement method.

Henderson, R., Jubb, J.S. & Rossmann, M.G.
J. Mol. Biol. 154, 501-514 (1982).
A contracted form of the trigonal purple membrane of Halobacterium halobium.

Henderson, R.
Nature, News and Views, 287, 490 (1980).
Crystallizing membrane proteins.

Deatherage, J.F., Henderson, R. & Capaldi, R.A.
In "Electron Microscopy at Molecular Dimensions", p. 91-100 (1980).
Eds. Baumeister, W. & Vogell, W.  Springer-Verlag, Berlin.  
Structure of cytochrome oxidase vesicle crystals.

Michel, H., Oesterhelt, D. & Henderson, R.
In "Electron Microscopy at Molecular Dimensions", p. 61-70 (1980).
Eds. Baumeister, W. & Vogell, W.  Springer-Verlag, Berlin.  
Formation of a new 2-D crystalline form of purple membrane.

Wallace, B.A., & Henderson, R.
In "Electron Microscopy at Molecular Dimensions", p. 57-60 (1980).
Eds. Baumeister, W. & Vogell, W.  Springer-Verlag, Berlin.
Diffraction studies of modified purple membrane.

Henderson, R.
In "Biophysics of Membranes and Intercellular Communication".  Les Houches Series, 33, 232-249 (1981) North Holland Publisher.  Eds. Chabre, M. & Devauz, P.
Membrane protein structure.

Engelman, D.M., Henderson, R., McLachlan, A.D. & Wallace, B.A.
Proc. Nat. Acad. Sci. U.S.A. 77, 2023-2027 (1980).
The path of the polypeptide in bacteriorhodopsin.

Henderson, R. & Shotton, D.M.
J. Mol. Biol. 139, 99-109 (1980).
Crystallisation of purple membrane in three-dimensions.

Michel, H., Oesterhelt, D. & Henderson, R.
Proc. Nat. Acad. Sci. U.S.A. 77, 338-342 (1980).
An orthorhombic two-dimensional crystal form of purple membrane.

Fuller, S.D., Capaldi, R.A. & Henderson, R.
J. Mol. Biol. 134, 305-327 (1979).
Structure of cytochrome c oxidase in deoxycholate derived two-dimensional crystals.

Henderson, R.
In "Membrane Transduction Mechanisms"  Soc. Gen. Physiol. Series Vol. 33, 3-15 (1979).  Eds. Cone, R.A. & Dowling, J. Raven Press, New York.
The structure of bacteriorhodopsin and its relevance to the structure of other membrane proteins.

Zingsheim, H.P., Henderson, R. & Neugebauer, D.-C.
J. Mol. Biol. 123, 275-278 (1978).
Properties of the two sides of purple membrane correlated.

Henderson, R., Jubb, J.S. & Whytock, S.
J. Mol. Biol. 123, 259-274 (1978).
Specific labelling of the protein and lipid on the extracellular surface of purple membrane.

Cherry, R.J., Müller, U., Henderson, R. & Heyn, M.P.
J. Mol. Biol. 121, 283-298 (1978).
Temperature-dependent aggregation of bacteriorhodopsin in DPL and DML vesicles.

Henderson, R.
Soc. Gen. Microbiol. Symposium 28, 225-230 (1978).
Eds. Stainer, R.Y., Rogers, H.J. & Ward, J.B., Cambridge Univ. Press.  
The purple membrane of Halobacteria.

Henderson, R. & Unwin, P.N.T.
Biophys. Struct. Mechanism. 3, 121 (1977).
Structure of the purple membrane from Halobacterium halobium.

Henderson, R., Capaldi, R.A. & Leigh, J.S.
J. Mol. Biol. 112, 631-648 (1977).
The arrangement of cytochrome oxidase molecules in two-dimensional vesicle crystals.

Henderson, R.
Ann. Rev. Biophys. Bioeng. 6, 87-109 (1977).
The purple membrane from Halobacterium halobium.

Unwin, P.N.T. & Henderson, R.
33rd Ann. Proc. Electron Microscopy Soc. Amer. p. 298-299 (1975) G.W. Bailey (Ed.)
High resolution structure determination of unstained biological molecules.

Henderson, R. & Unwin, P.N.T.
Nature 257, 28-32 (1975).
Three dimensional model of purple membrane obtained by electron microscopy.

Unwin, P.N.T. & Henderson, R.
J. Mol. Biol.  94, 425-440 (1975).
Molecular structure determination by electron microscopy of unstained crystalline specimens.

Henderson, R.
J. Mol. Biol.  93, 123-138 (1975).
The structure of the purple membrane from Halobacterium halobium:  analysis of the X-ray diffraction pattern.

Henderson, R. & Strichartz, G.R.
J. Physiol.  238, 329-342 (1974).
Ion fluxes through the sodium channels of garfish olfactory nerve membranes.

Henderson, R., Ritchie, J.M. & Strichartz, G.R.
Proc. Nat. Acad. Sci. USA 71, 3936-3940 (1974).
Evidence that TTX and STX act at a metal cation binding site in the sodium channels of nerve membrane.

Henderson, R., Ritchie, J.M. & Strichartz, G.R.
J. Physiol.  235, 783-804 (1973).
The binding of labelled saxitoxin to the sodium channels in nerve membranes.

Henderson, R. & Wang, J.H.
Biochemistry 11, 4565-4569 (1972).
Solubilisation of specific tetrodotoxin-binding component from garfish olfactory nerve membrane.

Colquhoun, D., Henderson, R. & Ritchie, J.M.
J. Physiol. 227, 95-126 (1972).
The binding of labelled tetrodotoxin to non-myelinated nerve fibres.

Henderson, R. & Wang, J.H.
Ann. Rev. Biophys. Bioeng. 1, 1-26 (1972).
Catalytic configurations.

Henderson, R., Wright, C.A., Hess, G.P. & Blow, D.M.
Cold Spring Harbor Symp. 36, 63-70 (1971).
α-chymotrypsin:  What can we learn about catalysis from X-ray diffraction?

Henderson, R.
Biochem. J. 125, 13-18 (1971).
Catalytic activity of α-chymotrypsin in which His-57 has been methylated.

Henderson, R. & Moffat, J.K.
Acta Cryst. B27, 1414-1420 (1971).
Difference Fourier technique in protein crystallography.

Henderson, R.
J. Mol. Biol. 54, 341-354 (1970).
Structure of crystalline α-chymotrypsin IV.  The structure of indoleacryloyl-α-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme.

Birktoft, J.J., Blow, D.M., Henderson, R. & Steitz, T.A.
Phil. Trans. Roy. Soc. B. 257, 67-76 (1970).
Serine proteinases.  The structure of α-chymotrypsin.

Steitz, T.A., Henderson, R. & Blow, D.M.
J. Mol. Biol. 46, 337-348 (1969).
Structure of crystalline α-chymotrypsin III. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin.

Sigler, P.B., Blow, D.M., Matthews, B.W. & Henderson, R.
J. Mol. Biol. 35, 143-164 (1968).
Structure of crystalline α-chymotrypsin II. A preliminary report including a hypothesis for the activation mechanism.

Matthews, B.W., Sigler, P.B., Henderson, R. & Blow, D.M.
Nature 214, 652-656 (1967).
Three-dimensional structure of Tosyl-α-chymotrypsin.