Biomolecule Imaging technique awarded Nobel Prize for Chemistry

By Ryan Jones Matthews

Widely considered the most prestigious accolade in science, the Nobel Prize is awarded to scientists whose work is considered an “outstanding contribution for humanity” in their respective fields. This year, the prize in Chemistry has been awarded to 3 European scientists for their work in developing a method to produce high-resolution three-dimensional models of biomolecules such as DNA.

The recipients of the award are Jacques Dubochet, a Swiss biophysicist at the University of Lausanne; Joachim Frank, a German professor of biochemistry and biophysics at Colombia University; and Richard Henderson, a British researcher at the MRC Laboratory of Molecular Biology in Cambridge. They will share a prize fund of 9 million Swedish Kroner (about £850,000).

The method, called cryo-electron microscopy, freezes biomolecules in mid-movement to perfectly preserve their physical shape and, using electron microscopes, makes previously invisible processes into precise atomic models.

The Nobel Foundation said the results of the technology are “decisive for both the basic understanding of life’s chemistry and the development of pharmaceuticals”.

It has already led to an increased understanding of viruses like Zika, which causes defects such as microcephaly in unborn children, and an epidemic of which spread through South America in 2015 and 2016.

Cryo-electron microscopy was first made conceivable by Professor Frank when, between 1975 and 1986, he developed an image-processing method where fuzzy two-dimensional images generated by electron microscopes are analysed and refined into sharp three-dimensional models.

Then, in the early 1980s, Professor Dubochet succeeded in vitrifying water. Vitrification is the process in where water is cooled down so rapidly that it solidifies in its liquid form around a biological sample. This allows biomolecules to keep their natural shape. Professor Dubochet’s work on water vitrification also helped to smash the long-held belief that electron microscopes were only suitable for taking images of dead matter.

Finally, in 1990, Dr. Henderson, using the revolutionary process developed by Dubochet, succeeded in generating a three-dimensional image of a living protein at atomic scale. Henderson’s breakthrough then proved the viability and potential of cryo-electron microscopy.

However, it took 23 years of refining and optimising electron microscopes before the technique could achieve the desired atomic resolution. Since 2013, thanks to Frank, Dubochet, and Henderson’s work, scientists and researchers have been able to routinely produce perfect three-dimensional models of biomolecules.

These models have been used to study everything from proteins that cause viruses to become resistant to antibiotics, to the building blocks of life itself – DNA and RNA. Thanks to cryo-electron microscopy, as Professor Sara Snogerup Linse, who chaired the Nobel committee for the Chemistry prize put it:Soon there will be no more secrets.”

Dr. Henderson, who received the phone call telling him he had won during a news briefing in Cambridge, also stressed the importance of others’ work in the development of the technique.

“I think the feeling is that the three of us who have been awarded the prize are sort of acting on behalf of the whole field,” he said. “It’s kind of a worldwide effort that’s just now come to fruition.”