This year’s highly coveted Nobel Prize in Chemistry has finally been awarded to a group of scientists who dedicated their work to the improvement of cryo-electron microscopy.
On Wednesday, Jacques Dubochet of Switzerland, Joachim Frank of the U.S. and Richard Henderson of the U.K. were awarded the Nobel Prize in Chemistry for developing a new way to create three dimensional (3D) images of biological molecules using cryo-electron microscopy.
— The Nobel Prize (@NobelPrize) October 4, 2017
In a press release published by the The Royal Swedish Academy of Sciences, the awarding body behind the Nobel Prize, they acknowledged the importance of the enhanced technique, known as cryo-electron microscopy, contributed by the three scientists in the fields of biochemistry. They wrote:
“We may soon have detailed images of life’s complex machineries in atomic resolution. The Nobel Prize in Chemistry 2017 is awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules. This method has moved biochemistry into a new era.”
The organization also emphasized that “picture is a key to understanding” and that scientific breakthroughs are often built upon the “successful visualization of objects invisible to the human eye.”
So, what made cryo-electron microscopy so vital that it won the Nobel Prize? Let’s find out!@NobelPrize finally awarded #NobelPrize in Chemistry this year to 3 scientists for their work in the improvement of cryo-electron microscopy!Click To Tweet
Cryo-electron Microscopy: Improving the Study of Biological Molecules
Cryo-electron microscopy (cryo-EM), also known as electron cryomicroscopy, is a form of transmission electron microscopy (TEM) which uses beams of electrons transmitted through specimens to form images. Cryo-EM is popular in structural biology where it is used to study samples at cryogenic temperatures.
Cryo-EM is specifically important in studying the biological molecules of specimens because it allows researchers to observe them in their native, unstained environments.
“A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualization of objects invisible to the human eye. However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery,” The Royal Swedish Academy of Sciences said.
“Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualize processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.”
Before, it was difficult for scientists to produce detailed images of many biomolecules such as DNA and RNA. The process often requires the usage of dyes or fixatives to help see the molecules. Electron microscopes were also used in getting images of dead materials only because the electron beams are destroying biological matter.
However, the development contributed by the trio in the advancement of cryo-electron microscopy enabled researchers today to freeze biomolecules mid-movement and observe how they act and interact with each other or with their environment.
Cryo-electron Microscopy: Early Studies and Development
It all started in the 1980s when Dubochet and his colleagues successfully vitrified water. He was able to cool the water so rapidly that it solidified in its liquid form around a biological sample which allows biomolecules to keep their natural shape.
During the same time, between 1975 and 1986, Frank developed an image processing method in which the electron microscope’s fuzzy two-dimensional images are analyzed and merged to reveal a fine three-dimensional structure.
Come 1990, Henderson succeeded in using the electron microscope to generate a three-dimensional image of protein at atomic resolution.
Following the three scientists discoveries, the electron microscope has been intensively optimized for better image capture. Since then, cryo-EM images and maps improved drastically. In 2013, near atomic structures of viruses (ZIKA), ribosomes, mitochondria, ion channels, and enzymes as small as 170 kDa were obtained at a resolution of 4.5.
The final technical hurdle was overcome in 2013, when a new type of electron detector came into use. pic.twitter.com/Ue9c0R6v7y
— The Nobel Prize (@NobelPrize) October 4, 2017
Apparently, all these development won’t be possible without the studies conducted by the three scientists.
Speaking at the conference by telephone, Frank explained that enhancements in cryo-electron microscopy “fills an important gap and extends the range of molecules that can be determined at atomic resolution.”
The awarding of the Nobel Prize in Chemistry to Frank, Dubochet, and Henderson, received positive reactions from the academic community of chemists since their contribution to the development of cryo-electron microscopy revolutionized the study of biomolecules.
“We are facing a revolution in biochemistry.”
Sara Snogerup Linse, Nobel Committee Chairman, was quoted as saying during the announcement. “Now we can see the intricate details of the biomolecules in every corner of our cells, in every drop of our body fluids. We can understand how they are built and how they act and how they work together in large communities.”
“To give one example, last year the 3D structure of the enzyme producing the amyloid (protein) of Alzheimer’s disease was published using this technology,” John Hardy, a professor of Neuroscience at the University College of London, added. “Knowing this structure opens up the possibility of rational drug design in this area.”
The Nobel Prize comes with a 9 million Swedish kronor ($1.1 million USD) reward that will be shared when there are multiple recipients. Other notable recipients of the Nobel Prize in Chemistry are Marie Curie for the discovery of the elements radium and polonium and John Pope for the development of computational methods in quantum chemistry.
The Nobel Prize in Chemistry is annually awarded by the Royal Swedish Academy of Sciences to scientists in various fields of chemistry. It was established in the 1895 will of Alfred Bernhard Nobel, a Swedish chemist, engineer, inventor, businessman, and philanthropist.