【Taiwan】

Three researchers who developed a way to see the basic molecules of life in three dimensions won the 2017 Nobel Prize in chemistry,Taiwan the Royal Swedish Academy of Sciences announced on Wednesday.

Jacques Dubochet of Switzerland’s University of Lausanne, Joachim Frank of Columbia University in New York City, and Richard Henderson of the MRC Laboratory of Molecular Biology in England were honored “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution,” said Göran Hansson, Secretary General of the Royal Swedish Academy of Sciences, in announcing the prize in Stockholm.

SEE ALSO: Google Doodle honours Australia's only Nobel Prize winner in chemistry

Basically, cryo-EM lets biologists see what they’re studying, from the surface of the Zika virus to human enzymes involved in disease. If a molecule involved in cancer, for instance, by seeing its shape drug developers can glean clues about the kind of molecule they need to create to disrupt the molecule. The prize is therefore another example of the chemistry Nobel honoring research that is squarely within biology.

The three scientists will receive the Nobel Medal, Nobel Diploma and a document confirming the Nobel Prize amount (9 million Swedish krona, about $1.1 million) from King Carl XVI Gustaf of Sweden at the annual Nobel ceremony in Stockholm on Dec. 10, along with the rest of this year’s laureates.

Cryo-electron microscopy, the Nobel committee said, “has moved biochemistry into a new era,” because “a picture is a key to understanding.”

Mashable Trend Report Decode what’s viral, what’s next, and what it all means. Sign up for Mashable’s weekly Trend Report newsletter. By clicking Sign Me Up, you confirm you are 16+ and agree to our Terms of Use and Privacy Policy. Thanks for signing up!

This Tweet is currently unavailable. It might be loading or has been removed.

“I think this is a very exciting choice,” Jeremy Berg, editor in chief of Scienceand former director of the National Institute for General Medical Sciences at the National Institutes of Health, told STAT. Cryo-EM “is truly revolutionizing biochemistry, particularly over the past five years.” Many of the structures it has revealed, often at an atomic level, “are those of greatest interest to biologists, but have been difficult to reveal by other means,” he said, including “ion channels central to the function of the nervous system and the machinery for splicing RNA, essential for effective gene expression.”

The three laureates worked independently, but their discoveries about how to prepare biological samples to have their picture taken, how to take the picture without destroying the sample, and how to turn the initial fuzzy image into something sharp converged to make cryo-EM today’s go-to imaging technology.

Older microscopic techniques couldn’t generate images of life’s molecular machines; the cutting edge technique of yore, electron microscopy, seemed to work only for seeing dead objects, since the electron beam destroys living things. But Frank, who said on Wednesday that he “didn’t mind” receiving the early-morning call from Stockholm, developed a way to take the fuzzy 2D images from electron microscopes and turn them into a sharp 3D picture, the first step toward cryo-EM.

(L-R) Swiss scientist Jacques Dubochet, German scientist Joachim Frank and British scientist Richard Henderson. Credit: UNIVERSITY LAUSANNE/COLUMBIA/CAMBRIDGE UNIVERSITY/EPA-EFE/REX/Shutterstock

Ordinary electron microscopy makes biomolecules, which contain water, collapse. But in the 1970s Dubochet showed that adding water to electron microscopy in a certain way that prevented that. He cooled water so rapidly that it became a sort of solid liquid (more like glass than ice, despite the “cryo” in the same), forming a sort of cage around the biological sample, letting the biomolecules keep their shape. (Dubochet is known not only for his discoveries but also for having one of science’s more unusual official CV‘s, which starts with being “conceived by optimistic parents” in October 1941 and includes “being the first official dyslexic in the canton of Vaud” in 1955.)

Henderson showed that it is possible to freeze biomolecules “mid-movement,” the Nobel committee said, generating a three-dimensional image of a protein down to the atomic level. His breakthrough came in 1990, when he used cryo-EM to reveal the 3D structure of a bacterial protein called bacteriorhodopsin. That demonstration of what cryo-EM could achieve was “decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals,” the committee said.

In the new millennium, cryo-EM became the go-to technology for seeing the molecules of life, capturing everything from proteins that cause antibiotic resistance to the surface of the Zika virus to receptors in human cells that sense the spiciness molecule in chili peppers. And biologists hope that by actually seeing what their drugs have to target, they might develop more effective medications more quickly: a study last year, for instance, showed the atomic-level structure of an enzyme that, if disrupted, might fight cancer.

---

Featured Video For You

---

The disturbing truth about vitamins

---