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Science: Nobel in chemistry for cryo-electron microscopy

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Cool way to peer into molecules’ inner workings wins chemistry Nobel Prize

Science News said:
An imaging technique that lets scientists capture 3-D views of proteins, viruses and other molecules at the atomic scale has won its developers the 2017 Nobel Prize in chemistry.

Jacques Dubochet of the University of Lausanne in Switzerland, Joachim Frank of Columbia University and Richard Henderson of the MRC Laboratory of Molecular Biology in Cambridge will share the prize, the Royal Swedish Academy of Sciences announced October 4.

Called cryo-electron microscopy, the imaging technique freezes biological molecules in place and reveals their inner workings.

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Here's a longer article on it:

Supercool Protein Imaging Gets the Nobel Prize

Quanta Magazine said:
Seeing is believing, but for creatures as visually oriented as humans, seeing is also understanding. Much of the past century’s progress in biology has come from scientists being able to picture what DNA helices, protein channels and other biomolecules look like within the milieu of the cell. This year’s Nobel Prize in Chemistry celebrates three scientists for their role in developing cryo-electron microscopy, a technique that literally freezes biomolecules in living cells in mid-motion and resolves their images down to the level of atoms.

Jacques Dubochet at the University of Lausanne in Switzerland, Joachim Frank at Columbia University and Richard Henderson at the MRC Laboratory of Molecular Biology in Cambridge will share the Nobel Prize for work they pursued separately over decades to improve the state of biological imaging. Cryo-electron microscopy, usually called cryo-EM for short, is the brainchild of their contributions and those of their colleagues.

Proteins and other biomolecules are essentially nanomachines, and any detailed understanding of them requires knowing with precision how they change shape, bond to other molecules and pass around ions while sitting in cell membranes or floating in solution. The challenge of seeing them that way goes beyond overcoming their tininess. Chemical fixatives and stains can immobilize biomolecules for microscopy but they typically alter the form and configuration of the molecules in the process. Conventional freezing doesn’t help: Ice crystals rupture cell membranes and push the proteins around; the biomolecules react faster than the water freezes; and evaporating ice crystals disrupt the fidelity of the images.

In the mid-20th century, scientists began to use standard electron microscopy, X-ray crystallography and nuclear magnetic resonance imaging to study biomolecules, and those techniques overcame some of the problems, particularly with revealing the desired level of fine structure. But all of them traded off those answers for some level of accurate information about how the molecules looked and behaved in living systems.

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