The work of Joachim Frank, left, and Richard Henderson in advancing cryo-electron microscopy allows researchers to freeze biomolecules midmovement, revealing the atomic structure of a sample. | From left, Columbia University Medical Center, MRC Laboratory of Molecular Biology
AAAS Fellow Joachim Frank and AAAS member Richard Henderson were awarded the 2017 Nobel Prize in Chemistry for developing a type of electron microscopy that provides detailed views of the structures of the smallest molecules of life, the Royal Swedish Academy of Sciences announced Oct. 4.
Frank of Columbia University, Henderson of the MRC Laboratory of Molecular Biology in Cambridge, England and Jacques Dubochet of the University of Lausanne in Switzerland were named Nobel laureates for significant discoveries that led to the development and use of cryo-electron microscopy to produce close-up, three-dimensional views of biomolecules.
“The method has taken biochemistry into a new era, making it easier than ever before to capture images of biomolecules,” said the Nobel committee in making the announcement from Stockholm.
The German-born Frank, who was inducted as a AAAS fellow in 1997, is a professor of biochemistry, molecular biophysics and biological sciences at Columbia in New York City and the Scottish-born Henderson, who has been a AAAS member since 1996, has served as director of the MRC Laboratory of Molecular Biology research facility where hundreds of scientists work on neurobiology, cell biology and biotechnology.
From laboratories in various parts of the world, the trio worked on the challenge of modifying and developing ways to expand the applications of the electron microscope. Eventually, they produced a three-dimensional image of a protein to reveal its working architecture, deepening scientific understanding of the processes at work – knowledge that has been used to develop pharmaceuticals.
In 1990, Henderson was the first to use an electron microscope to produce “a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential,” the committee said.
Over more than a decade beginning in 1975, Frank set out to develop ways to expand the microscopes’ reach to enable it to be applied to more molecules. “He developed an image processing method in which the electron microscope’s fuzzy two-dimensional images are analyzed and merged to reveal a sharp three-dimensional structure,” the committee explained.
In the 1980s, Dubochet got around a problem by developing a quick-freezing process that allowed water in cells to solidify, exposing each feature so it could be studied and examined.
Researchers have gone on to study “proteins that cause antibiotic resistance” and to produce three-dimensional images of the Zika virus at atomic resolution, permitting scientists to hunt for weaknesses that new pharmaceuticals could exploit.
The chemistry award was the final of three scientific disciplines the Nobel committee honored over three consecutive days.
On Oct. 3, three AAAS fellows were awarded the 2017 Nobel Prize in Physics for work that led to the first detection of gravitational waves by the Laser Interferometer Gravitational-wave Observatory in 2015.
A day before, the Nobel committee awarded two other AAAS members, one of whom is AAAS fellow, the 2017 Nobel Prize in Physiology or Medicine for uncovering the molecular mechanisms controlling the circadian rhythm of living creatures.