A scanning electron microscope. Image: Bildagentur Zoonar GmbH/Shutterstock
The 2017 Nobel Prize in Chemistry has been awarded to three researchers for their ‘cool’ solution to observing biomolecules.
Thanks to the work of Jacques Dubochet, Joachim Frank and Richard Henderson, our ability to see and understand the inner working of biomolecules has been vastly improved.
The three researchers were recently announced as the winners of the 2017 Nobel Prize in Chemistry for the development of cryo-electron microscopy.
Scientific breakthroughs often build upon the successful visualisation of objects invisible to the human eye, but for decades these biochemical maps have had large blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery.
With cryo-electron microscopy however, researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, revealing a whole new understanding of life’s chemistry and pharmaceutical manufacturing.
The defining breakthrough in the science was made by Henderson in 1990 who proved the technology’s potential by using an electron microscope to create a 3D image of a protein (bacteriorhodopsin) at atomic resolution.
3D structures of biomolecules. Image: Johan Jarnestad/The Royal Swedish Academy of Sciences
Until that moment electron microscopes were thought to only be good at imaging dead matter because the powerful electron beam destroys biological material.
It was Frank who, between 1975 and 1986, developed an image processing method in which the electron microscope’s fuzzy 2D images were analysed and merged to reveal a sharp 3D structure.
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 work of these three individuals helped put in place the milestone achieved in 2013 when the desired atomic resolution was reached, allowing scientists to produce 3D structures of biomolecules with ease.
This ability has significantly contributed to scientific advancements, the Nobel Prize Committee said, and has filled journals with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus.
