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MRC Scientist Wins 2017 Nobel Prize in Chemistry
Oct 06 2017 Read 1593 Times
Our congratulations go to Richard Henderson of the MRC’s Laboratory of Molecular Biology (LMB) who has been 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 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, the MRC were delighted to announce.
Born and educated in Scotland, Richard received a PhD at Cambridge then worked at Yale University before returning to the LMB where, since 1973, his work has helped to advance the use of 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. 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.
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.
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.”
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