The 2017 Chemistry Nobel Prize as been awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution.
Dr Ed Morris, Leader of the Structural Electron Microscopy Team at The Institute of Cancer Research, London, said:
“It is wonderful to hear the news that Jacques Dubochet, Joachim Frank and Richard Henderson have been awarded the 2017 Nobel prize in Chemistry for their work on cryo-electron microscopy. Cryo-electron microscopy is revolutionising molecular and cellular biology allowing the detailed understanding of the molecular machines within cells and how they work. This type of information is crucial, for example, in identifying new therapeutic targets and in designing drugs to treat diseases such as cancer. Dubochet, Frank and Henderson are each pioneers in the field and have conducted ground-breaking research over a number of years to bring cryo-electron microscopy to its current level. They each richly deserve the award, a prestigious and extremely timely recognition of an area of scientific research which is already transforming the way we look at the inner workings of cells.”
Dr Richard Henderson, joint winner of the 2017 Nobel Prize for Chemistry, said:
“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 with his method of rapid-freezing in the early 1980s, a crucial advance.”
Prof Sir John Savill, CEO of the Medical Research Council, which has funded Richard since 1973, 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.”
Prof. Dave Stuart, Director of Life Sciences at Diamond Light Sources and Professor of Structural Biology at Oxford University, said:
The team at Diamond congratulate Richard Henderson, Jacques Dubochet and Joachim Frank on being awarded the 2017 Nobel Prize in Chemistry. The cryo-electron microscopy (cryo-EM) community is in the throes of a ‘resolution revolution’, as predicted by Prof Henderson and collaborators. Their visionary work enables researchers to see in exquisite detail the structures of life, and cryo-EM is now rapidly maturing from a technique limited to a relatively small circle of expert users to one of very broad interest. Diamond are pleased to be part of the revolution by opening our national Electron Bio-Imaging centre (eBIC) to all.
Dr Andrea Sella, Professor of Inorganic Chemistry at UCL, said:
“In the minds of most people, the image of the scientist involves having a microscope somewhere: at some point “the scientist” peers into it and sees stuff – i.e. makes observations – directly. One of the reasons that chemistry has always been regarded as so difficult and abstract is the fact that one cannot actually see the atoms and molecules directly. Instead we rely on a complex code of formulas and stick diagrams.
“Yet over the past 200 years chemist have managed to infer an astonishing amount of information from clever chemical experiments that have involved converting one molecule into another. That really began to change in the early 20th century with the development of X-ray diffraction techniques that started to provide 3D structures of molecules of ever greater complexity. Perutz’s structure myoglobin, for example was one of the great triumphs. The problem is that this requires a crystal. And a molecule like myoglobin does not sit in a crystal. Like many proteins it is associated with other machinery in the cell and you are always left with the nagging doubt that the picture obtained by Perutz might not be exactly the same as the working molecule. And this is what transmission electron microscopy allows us to do. You can shine a bright beam of electrons through a sample, and in the same way as an old fashion slide projector, the image of the slide appears on the screen. By taking the temperatures very low and managing to pin down the water, the technique of cryo-TEM has really opened up the molecular world of the cell to direct observation. Not only can you see where molecules sit relative to each other, but the resolution has now improved so much that you can get pretty well down to the atomic level. This represents a remarkable change in the way in which we can study complex systems like this. And cryo-TEM is also having huge impacts in materials chemistry/science.
“My one regret this year is that John Goodenough has not been honoured for the invention of the lithium battery. In terms of benefit to mankind, the lithium battery has gone hand in hand with our technological shift to portable, wearable tech. But it is also having an enormous role in shifting our thinking about energy and how we handle it, in the face of climate change. Goodenough is 94 and time is running out.”
Prof. Anthony Watts, President of the European Biophysical Societies Association, said:
“Richard has been a pioneering and indefatigable spirit in biophysics for over 4 decades, and his seminal work on membrane protein structure determinations from the mid-1970s until now, has shaped the field. This recognition is long overdue and very well deserved, and adds to the long line of British biophysicists who have been recognized by the Nobel Committee”.
Dr Oliver Jones, Associate Professor of Analytical Chemistry at RMIT, Melbourne, said:
“As an analytical chemist it is great to see analytical methods win again at the Nobel’s this year. One might be forgiven for thinking that “surely microscopy is more physics than chemistry” but Cryo-EM is a great example of a technology that has enabled a huge amount of science, especially in biochemistry (which still counts as chemistry). I think it’s a very worthy winner. Congratulations to all involved”.
Prof Sir Venki Ramakrishnan, President of the Royal Society, said:
“I am delighted that Jacques Dubochet, Joachim Frank and Richard Henderson have jointly received a Nobel Prize. Their work has paved the way for the recent advances in electron microscopy that are revolutionising structural biology by making it possible to determine atomic structures of large macromolecules without the use of crystals.
“Richard Henderson, a Fellow of the Royal Society since 1983, is also a well-deserved recipient of last year’s Copley Medal – the world’s older scientific prize – not just for his ground-breaking work in electron microscopy but also his efforts in advancing and disseminating his ideas to the point where they have reached fruition and are now used prolifically across the world.
“The prize is also a testament to the value of decades of stable support for basic science by the MRC, which by revolutionising the way we see molecules is leading to advances in medicine. Congratulations.”
Dr Rob Kay, Group Leader, MRC Laboratory of Molecular Biology (LMB), said:
“This technique, long in the developing, has revolutionised structural biology allowing us to see the innermost workings of the tiny protein machines that run all of our cells. The prize could not be awarded to a more modest, constructive and deserving man. I am very happy.”
Dr Lucy Collinson, Head of Electron Microscopy at the Francis Crick Institute, says:
“Jacques Dubochet pioneered work on the process of vitrification – encasing cells and molecules in glassy ice – that meant that biologists could look at their samples close to their living state but at the atomic scale. Richard Henderson pioneered the development of the direct detector, a new type of camera that, when fitted to the electron microscope, can detect individual electrons – meaning that biologists can image proteins at the atomic scale. Joachim Frank pioneered the technique of cryo electron microscopy and single particle reconstruction – allowing biologists to image individual protein molecules at the atomic scale.
“Cryo electron microscopy has been revolutionised by the three Nobel prize winners, allowing molecules to be imaged at the atomic scale in a laboratory. Before the rapid developments in cryo EM pushed resolution to the atomic scale, researchers had to image their sample at a synchrotron using X-ray crystallography. Some samples are not amenable to X-ray crystallography, and cryo EM fills a gap for imaging many of these samples. Knowing the structure of individual molecules means that we can understand how they work, and ultimately design drugs to treat patients when these proteins go wrong. There has been huge uptake of the technique in the last five years, with cryo electron microscopes going into universities, institutes and pharma, and protein structures are now being published at an unprecedented rate.”
Prof Sir Hugh Pelham, Director of the MRC Laboratory of Molecular Biology, said:
“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.”
Prof Sir Colin Blakemore, Emeritus Professor of Neuroscience at the University of Oxford, said:
“This is wonderful news – for the UK, for the MRC, for the glorious MRC Laboratory of Molecular Biology in Cambridge – and for Richard, of course. This is the 11th Nobel Prize for one institute! (http://www2.mrc-lmb.cam.ac.uk/achievements/lmb-nobel-prizes/)
“Richard was the Director of the LMB for several years, during the complex planning of the new building. Despite the demands of that job, he continued his own remarkable science. He works on G-protein-coupled receptors (GPCRs). These are protein molecules in the membranes of cells that are stimulated by hormones, transmitters etc, and which work by activated so-called G-proteins that are linked to the receptor. In turn the G protein can turn on a variety of intracellular signalling pathways, to control the activity of the cell. GPCRs are very important in neurons. They are prime targets for drugs because of their involvement in a wide variety of diseases. But drug development depends on understanding the precise structure of the GPCR molecule. This proved to be extremely difficult and Richard had to develop new methods for doing this.”
Prof. Jim Smith, Director of Science at Wellcome, said:
“Warmest congratulations to Dubochet, Frank and Henderson for their Nobel Prize in Chemistry. Cryo Electron Microscopy is at the forefront of structural biology research, having undergone something of a resolution revolution in recent years. This prize recognises the contribution that the teams who developed cryo-EM have already made to research, and that it will continue to advance the field for many years to come. By solving more and more structures at the atomic level we can answer biological questions, such as how drugs get into cells, that were simply unanswerable a few years ago. Equipping UK researchers with the technology to undertake world-leading science is absolutely paramount, and Wellcome’s recent awards in this area will have far-reaching benefits across the life sciences.”
Prof Dame Anne Glover, President Elect of the Royal Society of Edinburgh, said:
“When I was doing my PhD, I remember visiting Richard at the MRC labs the day it was announced that Fred Sanger had won his second Nobel. Richard gave me great help with my PhD and ended up one of the examiners of my thesis. He was always happy to talk about ideas and to help so it is great that he has been awarded the Nobel for Chemistry.”
Prof. Michael Wakelam, Director of the Babraham Institute, said:
“An accomplished and highly-skilled scientist, Richard Henderson is a hugely deserving winner of the Nobel Prize for Chemistry. His ground-breaking work on developing cryo-electron microscopy and its use in solving the structures of proteins has been truly transformative in our understanding of biology. Richard has consistently made important contributions to science and the UK scientific community. I am proud to know him and grateful for his contributions to the Institute.”
Prof. Daniel Davis, British Society for Immunology spokesperson and Professor of Immunology at the University of Manchester, said:
“Cryo-electron microscopy is one of those techniques so basic and important that its use spans all of biology – including understanding the human body and human disease and in designing new medicines. Many of the key molecules and proteins that allow our immune system to work have been visualised in unprecedented detail with this technology. It has been used in visualising the way in which antibodies can work to stop viruses being dangerous, leading to new ideas for medicines – as just one example.”
Prof. Daniela Rhodes, NTU Institute of Structural Biology, Singapore, said:
“This is great news! Electron Microscopy is revolutionising structural biology and these three fully deserve the prize. Their contributions has opened up the field to researchers all over the world to determine the structure of huge machines in cells as well as smaller protein structures that will reveal how biology and medicine work. This is a well-deserved Nobel Prize!”
Prof. John Hardy, Professor of Neuroscience at UCL, said:
“The fantastic improvement in structural biology brought about through cryo-electron microscopy has been transformative. To give one example, last year the 3D structure of the enzyme producing the amyloid of Alzheimer’s disease was published using this technology. Knowing this structure opens up the possibility of rational drug design in this area. And as a biologist, I can say that the pictures are beautiful.”
Dr Luca Pellegrini from the Department of Biochemistry at the University of Cambridge said:
“We’re delighted about the news that the 2017 Nobel prize in Chemistry was jointly awarded to Dr Richard Henderson of the MRC Laboratory of Molecular Biology in Cambridge. The award recognises Dr Henderson’s long-standing interest in Electron Microscopy and its application to fundamental biological problems.
“The pioneering research carried out by Dr Henderson in the field of Electron Microscopy has revolutionised the structural investigation of biological specimens under native conditions, leading to a major breakthrough in our ability to obtain high-resolution images of macromolecular assemblies of biological and medical interest. “
Prof. Magdalena Zernicka-Goetz, Professor of Mammalian Development and Stem Cell Biology at the University of Cambridge, said:
“I think it is wonderful. A visual image is the essential component to understanding, often the first one to open our eyes, and so our minds, to a scientific breakthrough.”
Dame Carol Robinson, Professor of Chemistry at the Physical and Theoretical Chemistry Laboratory, Oxford University, said:
“I am delighted to see this research recognised in this way. It is truly transformative allowing us to see new images of biomolecules – I am personally very happy for Richard who predicted this would be possible many years previously.”