4 October 2017
The development of cryo-electron microscopy
(Credit: The Royal Swedish Academy of Sciences/Martin Hogborn)
British biochemist Professor Richard Henderson has today been awarded a Nobel Prize in Chemistry, alongside Professors Jacques Dubochet and Joachim Frank, for their pioneering work with cool microscope technology.
In recent years, the UK’s Science and Technology Facilities Council (STFC) has been working with Professor Henderson to continue the revolution in cryo-electron microscopy.
Professor Henderson, of the Medical Research Council’s (MRC) Laboratory of Molecular Biology, has been awarded the prize "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".
The research carried out by Professors Henderson, Dubochet and Frank, means we may soon have detailed images of life’s complex machineries in atomic resolution.
During the past decade, STFC and Professor Henderson have collaborated on the development of sensors for the cryogenic electron microscopy that he pioneered – supporting increased availability and impact of the technique.
Executive Director of STFC’s National Laboratories Dr Andrew Taylor said:
“Huge congratulations to Professors Richard Henderson, Joachim Frank and Jacques Dubochet for receiving the Nobel Prize in Chemistry 2017.
“It has been our privilege here at STFC to work with Professor Henderson to use our CMOS technologies to develop the latest generation of detectors for cryo-electron microscopy, and to support the collaboration developing the software needed to interpret these images.
“The Nobel Prize is thoroughly deserved. This work has already had a far-reaching impact in the field of biochemistry imaging the molecular machines that support life.”
Cryo-electron microscopy allows researchers to freeze biomolecules mid-movement and visualise processes not previously seen, which has a huge benefits for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.
Professor Frank first showed the technology could have wide applications in the 1970s, by creating an imaging processing method to turn the microscope’s two-dimensional images into a three-dimensional structure.
In the 1980s, Professor Dubochet successfully allowed biomolecules to retain their shape even in the electron microscope’s vacuum, by cooling water so rapidly it solidifies around the sample.
In 1990, Professor Henderson successfully used an electron microscope to generate a three-dimensional image of protein at atomic resolution. Previously, electron microscopes were only used to image dead matter as the powerful beam would destroy biological material. But Professor Henderson proved it could work.
Now researchers can now routinely produce three-dimensional structures of biomolecules.
In the last decade cryo-electron microscopy has undergone a ‘resolution revolution’ through direct detection of the microscope electrons. STFC’s CMOS imaging group have worked with Professor Henderson to develop the radiation hard sensors required for this. These sensors are now found in a number of the world’s leading electron microscopes such as those in the recently opened Bio Imaging Centre at the Diamond Light Source.
Using cryo-electron microscopy at the Bio Imaging Centre, researchers were recently able to create a new synthetic polio vaccine.
Today, the STFC’s Scientific Computing Department are part of a collaboration to nourish the community and support users and developers of the software employed in this field.