While the chemistry award has sometimes been overshadowed by the towering reputations of physics winners such as Albert Einstein, laureates include ground-breaking scientists such as radioactivity pioneers Ernest Rutherford and Marie Curie, though she also won the physics prize.
The award goes to three pioneers of a technique called cryo-electron microscopy: Jacques Dubochet of the University of Lausanne in Switzerland, Joachim Frank of Columbia University in New York City, and Richard Henderson of the Medical Research Council's Laboratory for Molecular Biology (LMB) in Cambridge, United Kingdom. They each take home a share of the SEK 9 million (EUR 945 000) award for their work with cryo-electron microscopy.
Committee chair Sara Snogerup Linse explained: "Soon, there are no more secrets, now, we can see the intricate details of the biomolecules in every corner of our cells and every drop of our body fluids".
To map the minute landscape of molecules, at scales as tiny as just tenths of a nanometer, and help decipher their functions, structural biologists have long relied on two tools: nuclear magnetic resonance, or NMR, spectroscopy and X-ray crystallography. The use of both techniques was, however, subject to limitations imposed by the nature of biomolecules.
"This method started in the biochemistry of a new era", said jury.
The Nobel Prize in Chemistry was award for developing cryo-electro microscopy.
Following the discoveries, the very nut and bolt of electron microscope have been optimized. You see how they work together. The second challenge is that the electron beam heats up and destroys delicate biological molecules.
Henderson worked with bacteriorhodopsin, a purple-colour protein embedded in a photosynthesising organism's membrane. They swapped water with a sugar cocktail, which could withstand the vacuum and systematically tweaked the settings of their microscope to limit the damage caused by the electrons. This can be addressed by using a weaker beam, but that would result in fuzzier images.
The new image (right) was taken at true atomic resolution. He created a way to capture the images of proteins and grouped them together via computer.
Another significant advance came from Dubochet in the early 1980s. In 1984, he published the first images of a number of different viruses, round and hexagonal, that are shown in sharp contrast against the background of vitrified water. "At the time that it was written, people thought it was a bit optimistic", says Peter Rosenthal of the Francis Crick Institute who did his postdoc with Henderson.
Frank's work between 1975 and 1986 proved that electron microscopes could be applied in general use.
Since then, the technique has been honed even further, improving its resolution.
The power of the technology could be seen in the Zika crisis previous year. The technique allows researchers to see the details of biological molecules like proteins, DNA, RNA, and viruses in ways that were impossible before. As electron microscopes have improved over the intervening years (in part thanks to Henderson's efforts) cryo-electron microscopy can now image biological molecules at the atomic level.
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