The Nobel Prize in Chemistry 2017 has been awarded to three researchers, Jacques Dubochet, Joachim Frank & Richard Henderson, for their work on imaging the molecules of life. The three winners of the $1.1 million (9 million kronor) prize adapted another technique, electron microscopy, which uses a beam of electrons rather than ordinary light to inspect samples.
"We are facing a revolution in biochemistry", said Nobel Committee chair Sara Snogerup Linse, a scientist a the Center for Molecular Protein Science at Lund University in Sweden.
"I think this is a very exciting choice", Jeremy Berg, editor in chief of Science and former director of the National Institute for General Medical Sciences at the National Institutes of Health, told STAT. Cryo-EM "is truly revolutionizing biochemistry, particularly over the past five years". The award, he says, "recognizes people who've done science for science's sake...." The use of both techniques was, however, subject to limitations imposed by the nature of biomolecules. By 1975, he had created a 3-dimensional picture of the protein. "It has been used in visualising the way in which antibodies can work to stop viruses being risky, leading to new ideas for medicines as just one example", said Daniel Davis, professor of immunology at the University of Manchester.
As electron microscopes improved, Henderson was eventually able to deduce the structure at the atomic scale by 1990 - showing that it was possible to do high-quality studies of biological molecules using an electron microscope.
Put together, these developments set the stage for what would become known as cryo-electron microscopy, with "cryo" being the prefix for "cold". "It underpins every [cryo-electron microscopy] experiment since". Henderson's sugar cocktail worked for things that dissolved readily in water, but less well for hydrophobic biomolecules like fats, lipids and some proteins. Pictures were taken from many different angles of the same membrane under the electron microscope to produce a rough 3D model of bacteriorhodopsin's structure. You see how they work together. The pattern of those deflections sketches out the material's atomic structure. They swapped water with a sugar cocktail, which could withstand the vacuum and systematically tweaked the settings of their microscope to limit the damage caused by the electrons.
But the image didn't yet have the resolution Henderson wanted.
Frank's image analysis for 3D structures.
Trump slams mayor of San Juan, Puerto Rico over hurricane relief effort
At least half of the bank branches in Puerto Rico are still not open, according to the Association of Banks of Puerto Rico . Trump and Vice President Pence are slated to visit the island next week. "We will quickly act on that request", Ryan said.
One such advance came from Frank, who was tackling the issue of orientation. The problem is that these collections of molecules yield a confusing assortment of images, as they are oriented randomly.
The work essentially deals with capturing extremely high-resolution images of a biomolecules. Do it too slowly and the water in the sample will turn into ice crystals that destroy the protein molecules.
Dubochet entered the fray in the 1980s by creating a faster method for cooling water. He published the first images of viruses suspended in water with this technique in 1984. That made the technology generally applicable. But for some time, the resolution of the images remained unsatisfying enough that many researchers called it "blobology".
Since then, the technique has been honed even further, improving its resolution.
The core challenge of ensuring that the biomolecule samples were not dehydrated, and did not collapse in the vacuum of cryo-EM imaging under the electron beam, was resolved by Jacques Dubochet. "They've opened up a completely new world to us, to see these molecules in the cell and how they interact", Peter Brzezinski, a biochemist at Stockholm University, said at this morning's announcement in the Swedish capital.
The power of the technology could be seen in the Zika crisis past year.
It has laid bare never-before-seen details of the tiny protein machines that run all cells.