Biochem boffins win the Nobel Prize for cryo-electron microscopy

Fancy method captures three-dimensional images of biomolecules

3D structures of proteins (Image credit: The Royal Swedish Academy of Sciences)

The 2017 Nobel Prize in Chemistry has been awarded to a trio of researchers that have developed a new technique that captures three dimensional images of biological molecules.

Jacques Dubochet, an honorary professor at the Swiss University of Lausanne, Joachim Frank, a professor at New York's Columbia University and Richard Henderson, an academic from the UK's Medical Research Council Laboratory of Molecular Biology will equally share the prize of 9m Swedish krona, roughly £839,176 ($1,111,344).

The method dubbed “cryo-electron microscopy” (cryo-EM) allows “high-resolution structure determination of biomolecules in solution” at the atomic level.

It’s particularly useful for seeing proteins, many of which are less the width of human hair, that are not well suited to other imaging techniques like x-ray crystallography. Proteins are suspended in a tiny drop of solution that is frozen close to -196oC (-321 oF), and an electron gun shoots electrons at the sample.

Some of the electrons are scattered away when they bump into the protein molecules, and some pass straight to a photodetector on the other side. This leaves a “shadow image” of the protein that gives information about its structure in two-dimensions.

Since the proteins in the icy solution will be frozen at different orientations, researchers can collect these images and begin to build a model of how the molecule looks in three-dimensions.

Speaking about the award, Henderson said on Wednesday: “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 early1980s with his method of rapid freezing to make a specimen of amorphous ice, a crucial advance.”

Being able to see strands of proteins in all their complex, threaded beauty will help scientists understand the biochemical processes and design more effective drugs. ®


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