Earlier this week, on October 4th, Jacques Dubochet, Joachim Frank, and Richard Henderson were awarded the Nobel Prize in Chemistry for their pioneering work in developing cyro-electron microscopy (cryo-EM), a technique that fires beams of electrons at proteins that have been frozen in solution, to deduce the biomolecules’ structure.
Before this discovery, X-ray crystallography has been used by biologists for decades to image biomolecular structures, by blasting X-rays at crystallized proteins. However, this method was usually only useful in imaging dead material due to electron beams destroying the biological matter. But thanks to cyro-EM, labs are excited at the opportunity to adopt the method, because it is able to take pictures of proteins that can’t easily be formed into large crystals.
The Royal Swedish Academy of Sciences (who awards the Nobel Prize of Chemisty every year) says the new implementation has “moved biochemistry into a new era.”
This new way of visualizing biomolecules, like in bacteria and viruses, can be examined under a microscope in their native, undamaged state. This technology has already been put to work making strides in helping to understand Alzheimer’s disease. Last year the 3D structure of the enzyme producing the protein of the disease was published using cyro-EM.
This method is also predicted to help open up the possibilities of rational drug design. The Nobel committee went on to say that this development is “decisive for both the basic understand of life’s chemistry and the development of drugs.”
Before cyro-EM, scientists were unable to produce detailed images of many biological molecules—the building blocks of life. This development is thought to reveal almost all secrets of the intricate details of biomolecules in every corner of our cells, in every drop of bodily fluid.
Nobel Committee Chairman, Sara Snogerup Linse commented that, “We can [begin] to understand how [biomolecules] are built and how they act and how they work together in large communities.”
Previous techniques included the use of dyes or fixatives to help see these same molecules. Now researchers can freeze biomolecules mid-movement and observe how they act and interact.
One of the winners, Joachim Frank, a biophysicist at Columbia University in New York City, told journalists that technological innovations can have a larger impact than discoveries. “Cryo-electron microscopy is about to completely transform structural biology.” He added that the development “fills an important gap and extends the range of molecules that can be determined at atomic resolution.”
The prize comes with a coin bag of 9 million Swedish kronor ($1.1 million), which is shared between the multiple recipients.
Past winners of the prestigious Nobel Prize in Chemistry include Marie Curie for her work on radioactivity, and Frederick Sanger, who was the only person to be awarded the Chemistry Prize twice, in 1958 and 1980.
Since Alfred Nobel began this tradition in 1901, 109 Nobel Prizes in Chemistry have been awarded. According to the Nobel Prize webpage, Chemistry was the most important science for Nobel’s own work. Many of his inventions and industrial processes he developed was based on chemical knowledge. Chemistry was the second prize area that Nobel mentioned in his will.