Cambridge molecular scientist shares Nobel chemistry prize
Richard Henderson of MRC Laboratory of Molecular Biology in Cambridge shares the £830,000 prize.
A British scientist has received a share of the Nobel Prize in Chemistry for helping to pioneer a “revolutionary” technique for studying the molecular machinery of life.
Dr Richard Henderson, from the MRC Laboratory of Molecular Biology in Cambridge, and his two fellow laureates were honoured for the development of cryo-electron microscopy (cryo-EM).
The technique allows scientists to freeze moving biomolecules such as proteins and visualise the intricate chemical processes that make life possible.
The other winners are Professor Jacques Dubochet from the University of Lausanne in Switzerland and Professor Joachim Frank from Columbia University in New York.
Each receives an equal share of the nine million Swedish krona (£837,000) prize money.
Electron microscopes were once thought to be useful only for examining non-living objects because their electron beams destroy biological material.
Freezing at very low temperatures provided a solution to the problem by protecting the examined material from damage.
Dr Henderson’s critical contribution to the emerging field came in 1990 when he succeeded in using an electron microscope to generate a three-dimensional image of a protein.
Colleagues said his reaction to learning of the award was typically modest.
He said: “I am delighted for everybody in the field that the Nobel Prize in Chemistry has been awarded to acknowledge the success of cryo-EM.
“I am particularly pleased that Jacques Dubochet has been recognised as the key person who kick-started the field with his method of rapid-freezing in the early 1980s, a crucial advance.”
Prof Frank laid the early foundations of cryo-EM between 1975 and 1986 when he developed a method of processing fuzzy two dimensional electron microscope images and turning them into sharply focused 3D structures.
Meanwhile Prof Dubochet introduced his method of vitrifying water – cooling water so rapidly that it solidifies around a biological sample, allowing the molecules to retain their natural shape even in a vacuum.
Explaining the significance of cryo-EM, Nobel chemistry committee member Heiner Linke said it allowed scientists to “see down to the position of individual atoms to be able to see how these molecules interact with one another, what complexes they build, how these complex machineries work”.
He added: “It’s really the first time that we can see biological molecules in their natural environment and how they actually work together down to the individual atoms.”
Today scientists routinely visualise the three-dimensional structure of biomolecules, imaging everything from the bacterial proteins that cause antibiotic resistance to the surface of the Zika virus.