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Image credit: MRC LMB

MRC scientist wins 2017 Nobel Prize in Chemistry

4 Oct 2017

The MRC is delighted to congratulate the MRC Laboratory of Molecular Biology’s (LMB) Dr Richard Henderson on being awarded the 2017 Nobel Prize in Chemistry, alongside Professor Jacques Dubochet and Dr Joachim Frank (LMB alumnus) “for developing cryo-electron microscopy (cryo-EM) for the high-resolution structure determination of biomolecules in solution.”

This is the eleventh Nobel Prize awarded for work undertaken at the LMB, which has rightly earned the nickname of ‘the Nobel Prize factory’. Since its establishment over 100 years ago, the total number of Nobel prizes awarded to MRC-funded scientists is now 23. Richard will receive his Nobel Prize in Sweden in December.

Richard was born and educated in Scotland. Following a PhD in Cambridge he worked at Yale University before returning to the LMB where he has been working since 1973 on using electron microscopy to solve complex membrane protein structures. Together with Nigel Unwin he successfully determined the first structure of 2-D crystals of the membrane protein bacteriorhodopsin using electron microscopy in 1975. Work over Richard’s career has helped to advance the technique of electron microscopy, which bombards proteins or other large biological molecules with electrons rather than X-rays, so that the atomic structure of proteins can be determined. This has allowed us to see the structure of large, flexible and complex proteins, which have been impossible to analyse by traditional X-ray crystallography techniques.

In the 1990s, Richard realised that it would be theoretically possible to extract enough signal from randomly dispersed molecules using electron microscopy to obtain their detailed atomic structures. This insight and Richard’s drive and determination over the next two decades led to the development of better detectors for electron microscopes and better software to analyse the images. This revolutionised the technique of cryo-EM, which involves flash-cooling molecules in a thin layer of aqueous solution before imaging them, a crucial method invented by Jacques Dubochet and his colleagues in the early 1980s. Computational processing the images is a key step, to which Joachim Frank made major early contributions.

In the last few years, there has been a quantum step forward in these imaging techniques, due to better microscopes, better electron detectors and better computer programs for calculating the structure from the images. These improvements are now allowing atomic structure determinations of many protein and other macromolecular assemblies that were previously very difficult or impossible to obtain. The new structures provide important insights into the biological function of the assemblies and, by catalysing the subsequent development of new diagnostic or therapeutic tools, should help to improve the health and wealth of the country.

Richard has been presented with many awards for his work and was recently awarded the Gjonnes Medal in electron crystallography by the International Union of Crystallography. He is a Fellow of the Royal Society and the Academy of Medical Sciences, and was Director of the LMB from 1996-2006.

On winning the Nobel Prize, Richard commented: “I am delighted for everybody in the field that the Nobel Prize for Chemistry has been awarded to acknowledge the success of cryo-EM. I am particularly pleased that Jacques Dubochet has been recognised as the key person who kick-started the field in the early 1980s with his method of rapid freezing to make a specimen of amorphous ice, a crucial advance.”

Professor Sir John Savill, CEO of the MRC, said: “We’re delighted to congratulate Dr Richard Henderson on being awarded the 2017 Nobel Prize in Chemistry, for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution. In his ground-breaking work over decades at the MRC Laboratory of Molecular Biology he has helped solve a number of the technical and conceptual problems which limited electron crystallography and by 1990, he and his colleagues succeeded in obtaining through EM analysis the first three-dimensional image of a protein at atomic resolution. This Nobel prize is a wonderful recognition of his tireless efforts in developing and applying cutting-edge technologies to challenging and important structural biology questions.

“Determining the structure of proteins in humans is critical to understanding how they interact in the body and developing better drugs for diseases. Cryo-EM is already producing huge advances in our ability to obtain the structure of proteins that are critical in many diseases, such as the recent discovery of the structure of tau protein filaments in Alzheimer’s disease.

“The MRC is proud to have funded Richard since 1973 and his research is a testament to the MRC’s strategy for long-term investment in basic research at the MRC Laboratory of Molecular Biology which has already attracted ten Nobel prizes.”

Professor Sir Hugh Pelham, Director of the MRC Laboratory of Molecular Biology, commented: “My warmest congratulations to Richard Henderson as well as Jacques Dubochet and Joachim Frank. This is a fantastic recognition of very many years of work developing this technology, which is already helping to solve key problems related to human health. It is incredible what can now be done. The impact will be profound and I am proud that the MRC Laboratory of Molecular Biology has played such a central role in this.”

Watch the press conference with Dr Richard Henderson and Professor Sir Hugh Pelham

For more information about cryo-EM, please see the following video:


  • Categories: Research
  • Health categories:
  • Locations: Cambridge
  • Type: News article, Success story