Former NERSC PI Wins Nobel Prize in Chemistry for Cryo-EM

Former NERSC PI Wins Nobel Prize in Chemistry for Cryo-EM

Former NERSC PI Wins Nobel Prize in Chemistry for Cryo-EM

The Royal Swedish Academy of Sciences said in a statement that "the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules, has moved biochemistry into a new era".

Three European-born scientists were awarded the Nobel Prize in Chemistry for developing a new way to precisely develop three-dimensional images of biological molecules like proteins, DNA and RNA.

The 2017 Nobel Prize in chemistry goes to Jacques Dubochet from Switzerland, Joachim Frank from the US and Richard Henderson from Britain, during an announcement at the Royal Swedish Academy of Sciences in Stockholm on Wednesday.

John Savill, professor and CEO at the United Kingdom government-funded Medical Research Council, said electron microscopy has enabled scientists to examine disease molecules up close.

Dubochet "worked to essentially start it, kicked off the field; he invented this method of making specimens we now use", Henderson said.

Image showing the difference in resolution that has been made possible by their breakthroughs.

Speaking by phone, Frank told a news conference after the Nobel announcement Wednesday that the method, called cryo-electron microscopy, meant medicine no longer focuses on organs but "looks at the processes in the cell".

It has laid bare never-before-seen details of the tiny protein machines that run all cells.

Then it was Dubochet who added water to the electron microscope and in the 1980s succeeded in cooling water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum. The award brings a 9 million Swedish crown ($1.1 million) prize.

Chemistry is the third of this year's Nobel Prizes.

Indeed, cryo-electron microscopy is already delivering results, such as the recent discovery of the structure of tau protein filaments in Alzheimer's disease.

The desired atomic resolution was reached in 2013, and researchers can now routinely produce 3D structures of biomolecules, the Academy said.

"Normally what I'd do if I was in Cambridge, we will have a party around tea-time in the lab but I expect we'll have it tomorrow instead", Henderson said.

Understanding the structure of proteins and working out how they interact in the body should spark fresh approaches to drug development, just as earlier advances had produced today's multibillion-dollar biotech drugs, he added.

The new technology is useful in taking pictures of live bio-molecules by freezing them while in motion.

Together with Nigel Unwin he successfully determined the first structure of 2-D crystals of the membrane protein bacteriorhodopsin using electron microscopy in 1975.

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