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The Nobel Prize in Chemistry 2017 was awarded to Jacques Dubochet, Joachim Frank and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".
Cool microscope technology revolutionises biochemistry
We may soon havedetailed images of life’s complex machineries in atomic resolution. The NobelPrize in Chemistry 2017 is awarded to Jacques Dubochet, Joachim Frank andRichard Henderson for the development of cryo-electron microscopy, whichboth simplifies and improves the imaging of biomolecules. This method has movedbiochemistry into a new era.
A picture is a keyto understanding. Scientific breakthroughs often build upon the successfulvisualisation of objects invisible to the human eye. However, biochemical mapshave long been filled with blank spaces because the available technology hashad difficulty generating images of much of life’s molecular machinery.Cryo-electron microscopy changes all of this. Researchers can now freezebiomolecules mid-movement and visualise processes they have never previouslyseen, which is decisive for both the basic understanding of life’s chemistryand for the development of pharmaceuticals.
Electronmicroscopes were long believed to only be suitable for imaging dead matter,because the powerful electron beam destroys biological material. But in 1990,Richard Henderson succeeded in using an electron microscope to generate athree-dimensional image of a protein at atomic resolution. This breakthroughproved the technology’s potential.
Joachim Frank madethe technology generally applicable. Between 1975 and 1986 he developed animage processing method in which the electron microscope’s fuzzy twodimensionalimages are analysed and merged to reveal a sharp three-dimensional structure.
Jacques Dubochetadded water to electron microscopy. Liquid water evaporates in the electronmicroscope’s vacuum, which makes the biomolecules collapse. In the early 1980s,Dubochet succeeded in vitrifying water – he cooled water so rapidly that itsolidified in its liquid form around a biological sample, allowing thebiomolecules to retain their natural shape even in a vacuum.
Following thesediscoveries, the electron microscope’s every nut and bolt have been optimised.The desired atomic resolution was reached in 2013, and researchers can nowroutinely produce three-dimensional structures of biomolecules. In the past fewyears, scientific literature has been filled with images of everything fromproteins that cause antibiotic resistance, to the surface of the Zika virus.Biochemistry is now facing an explosive development and is all set for anexciting future.
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