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Noble Prize in Chemistry 2017 goes to Method for visualising Biomolecules
The Nobel Prize in Chemistry 2017 has been awarded to Jacques Dubochet, Joachim Frank and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".

Prize amount: 9 million Swedish krona, to be shared equally between the Laureates.

Fllowing is the press release information as published on

Quote:A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualisation of objects invisible to the human eye.

However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery.

Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material. But in 1990, Richard Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy twodimensional images are analysed and merged to reveal a sharp three-dimensional structure

Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.

Following these discoveries, the electron microscope’s every nut and bolt have been optimised. The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus. Biochemistry is now facing an explosive development and is all set for an exciting future.

Attaching the Scientific Background of the research as well:

Sunil Nagpal
MS(Research) Scholar, IIT Delhi (Alumnus)
Advisor for the Biotech Students portal (
Computational Researcher in BioSciences at a leading MNC

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How does it can help in biology? Its just inquisitiveness
(10-05-2017, 09:16 PM)vishu272 Wrote: How does it can help in biology? Its just inquisitiveness

This technique which is called cryo-electron microscopy, allow biomolecules to be visualised in their natural configuration for the first time, triggering a revolution in biochemistry. The latest versions of the technology mean scientists can record biochemical processes as they unfold in film-like sequences.

Earlier imaging techniques, such as X-ray crystallography, required samples to be studied in a rigid state, revealing little about the dynamics of proteins and enzymes – many of which could not be successfully crystallised in any case. Another microscopic technique, the electron microscope, was only suitable for imaging dead matter, because its powerful beam destroyed delicate biological structures.

Cryo-electron microscopy has allowed scientists to explore the architecture of everything from the proteins that cause antibiotic resistance to the surface of the Zika virus. Last year the 3D structure of the enzyme producing the amyloid of Alzheimer’s disease was published using this technology. By capturing snapshots of the same system at different time-points, scientists can even stitch together jittery film sequences of biological processes as they unfold.

This has paved the way for both new basic insights into life’s chemistry and for the development of pharmaceuticals.

Lavkesh Sharma
Biotechnology Student

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