Cryo-electron microscopy Current Affairs - 2019
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The Royal Swedish Academy of Sciences has selected Jacques Dubochet, Joachim Frank and Richard Henderson for the 2017 Nobel Prize in Chemistry.
They were selected for developing cryo-electron microscopy for the high resolution structure determination of biomolecules in solution. Chemistry was third of this year’s Nobel Prizes.
Contributions of trio
Richard Henderson in 1990 was successful in using an electron microscope to generate a 3D image of a protein at atomic resolution. Joachim Frank made technology more widely applicable. Jacques Dubochet had helped with vitrification of water, which ensured that biological sample retained its natural shape even in vacuum and while frozen.
The Cryo-electron microscopy is specific type of electron microscopy based on principle of forming three-dimensional (3D) image by collecting and combining thousands of projections of biomolecules. Using it, researchers can now freeze mid-movement of biomolecules and can visualise processes they have never seen.
It helps to make it possible to see biomolecules in 3D after rapidly freezing them at -150°C (i.e. at cryogenic temperature), preserving their natural shape. It can reveal the structure of the molecules of life in exquisite detail. It is decisive for both basic understanding of chemistry and for development of pharmaceuticals.
Significance: Cryo-electron microscopy gives scientists opportunity to look at machinery of life in 3D form. This was not possible with earlier forms of electron microscopes as more powerful beams would destroy biological matter. It allows the study of fine cellular structures, viruses and protein complexes at molecular resolution.