Three&nbsp;scientists&nbsp;have&nbsp;shared the&nbsp;2017&nbsp;Nobel&nbsp;Prize&nbsp;in&nbsp;Chemistry, the Royal Swedish Academy of Sciences announced on Wednesday.

The&nbsp;Nobel&nbsp;Prize&nbsp;in&nbsp;Chemistry&nbsp;2017&nbsp;was awarded to&nbsp;Jacques&nbsp;Dubochet,&nbsp;Joachim&nbsp;Frank&nbsp;and Richard&nbsp;Henderson&nbsp;&quot;for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution&quot;.

Richard&nbsp;Henderson, born 1945 in Edinburgh, Scotland, is a Programme Leader at MRC Laboratory of Molecular Biology, Cambridge, UK.

In 1990,&nbsp;Henderson&nbsp;succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology&#39;s true potential.

Joachim&nbsp;Frank, born 1940 in Siegen, Germany, is a Professor of Biochemistry&nbsp;and Molecular Biophysics and of Biological Sciences at Columbia University, US.

Between 1975 and 1986&nbsp;Frank&nbsp;developed an image processing method in which the electron microscope&#39;s fuzzy two-dimensional images are analyzed and merged to reveal a sharp three-dimensional structure.

Jacques&nbsp;Dubochet, born 1942 in Aigle, Switzerland, is the Honorary Professor of Biophysics at University of Lausanne, Switzerland.

In the early 1980s,&nbsp;Dubochet&nbsp;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.

Thanks to the&nbsp;2017&nbsp;Nobel&nbsp;Prize&nbsp;winners in&nbsp;Chemistry, researchers can now freeze biomolecules mid-movement and visualize processes they have never previously seen, which is decisive for both the basic understanding of life&#39;s&nbsp;chemistry&nbsp;and for the development of pharmaceuticals, according to a statement released by the Royal Swedish Academy of Sciences.

The development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules, has moved biochemistry&nbsp;into a new era, the statement added.

&quot;It means that we add another tool for describing what they say the molecules of life, and for them, you could say practical applications, it means another tool to develop new drugs and new therapeutics for, I would say, any number of diseases that you could imagine, because for all of the diseases, of course, something goes wrong inside our bodies, and there is almost always possible to identify a protein or a set of processes that are not functioning well, and maybe then there will be new drugs developed that will help those processes, and for that, you need to know how molecules interact with one another, how they bind to one another, and this is what this method can give new insights into,&quot; said Astrid Graslund, member of the Royal Swedish Acadamy of Sciences.

This year&#39;s&nbsp;prize&nbsp;is 9 million SEK (1.1 million US&nbsp;dollars) and will be&nbsp;shared by the three laureates.

The?Nobel?Prize?in?Chemistry?2017?was awarded to?Jacques?Dubochet,?Joachim?Frank?and Richard?Henderson?'for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution'

Three scientists have shared the 2017 Nobel Prize in Chemistry, the Royal Swedish Academy of Sciences announced on Wednesday. The Nobel Prize in Chemistry 2017 was awarded to Jacques Dubochet, Joachim Frank and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution". Richard Henderson, born 1945 in Edinburgh, Scotland, is a Programme Leader at MRC Laboratory of Molecular Biology, Cambridge, UK. In 1990, 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 true potential. Joachim Frank, born 1940 in Siegen, Germany, is a Professor of Biochemistry and Molecular Biophysics and of Biological Sciences at Columbia University, US. Between 1975 and 1986 Frank 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. Jacques Dubochet, born 1942 in Aigle, Switzerland, is the Honorary Professor of Biophysics at University of Lausanne, Switzerland. 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. Thanks to the 2017 Nobel Prize winners in Chemistry, researchers can now freeze biomolecules mid-movement and visualize processes they have never previously seen, which is decisive for both the basic understanding of life's chemistry and for the development of pharmaceuticals, according to a statement released by the Royal Swedish Academy of Sciences. The development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules, has moved biochemistry into a new era, the statement added. "It means that we add another tool for describing what they say the molecules of life, and for them, you could say practical applications, it means another tool to develop new drugs and new therapeutics for, I would say, any number of diseases that you could imagine, because for all of the diseases, of course, something goes wrong inside our bodies, and there is almost always possible to identify a protein or a set of processes that are not functioning well, and maybe then there will be new drugs developed that will help those processes, and for that, you need to know how molecules interact with one another, how they bind to one another, and this is what this method can give new insights into," said Astrid Graslund, member of the Royal Swedish Acadamy of Sciences. This year's prize is 9 million SEK (1.1 million US dollars) and will be shared by the three laureates.

Scientists Jacques Dubochet, Joachim Frank, Richard Henderson share 2017 Nobel Prize in chemistry

A revolutionary technique dubbed cryo-electron microscopy, which has shed light on the Zika virus and an Alzheimer&#39;s enzyme earned scientists Jacques Dubochet, Joachim Frank and Richard Henderson the Nobel Chemistry Prize on Wednesday.

Thanks to the international team&#39;s &quot;cool method&quot;, which uses electron beams to examine the tiniest structures of cells, &quot;researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen,&quot; the Nobel chemistry committee said.

This has been &quot;decisive for both the basic understanding of life&#39;s chemistry and for the development of pharmaceuticals,&quot; it added.&nbsp;

The ultra-sensitive imaging method allows molecules to be flash-frozen and studied in their natural form, without the need for dyes.

It has laid bare never-before-seen details of the tiny protein machines that run all cells.

&quot;When researchers began to suspect that the Zika virus was causing the epidemic of brain-damaged newborns in Brazil, they turned to cryo-EM (electron microscopy) to visualise the virus,&quot; the committee said.&nbsp;

Frank, a 77-year-old, German-born biochemistry professor at Columbia University in New York, was woken from his sleep when the committee announced the prize in Stockholm, six hours ahead.

&quot;There are so many other discoveries every day, I was in a way speechless,&quot; he said. &quot;It&#39;s wonderful news.&quot;&nbsp;

In the first half of the 20th century, biomolecule, proteins, DNA and RNA, were terra incognita on the map of biochemistry.&nbsp;

Because the powerful electron beam destroys biological material, electron microscopes were long thought to be useful only to study the dead matter.&nbsp;

Tea party to celebrate

But 72-year-old Henderson, from the MRC Laboratory of Molecular Biology in Cambridge, used an electron microscope in 1990 to generate a three-dimensional image of a protein at atomic resolution, a groundbreaking discovery which proved the technology&#39;s potential.

Frank made it widely usable between 1975 and 1986, developing a method to transform the electron microscope&#39;s fuzzy two-dimensional images into sharp, 3-D composites.

Dubochet, today an honorary professor of biophysics at the University of Lausanne, added water.

Now 75, he discovered in the 1980s how to cool water so quickly that it solidifies in liquid form around a biological sample, allowing the molecules to retain their natural shape even in a vacuum.

The electron microscope&#39;s every nut and bolt have been optimised since these discoveries.&nbsp;

The required atomic resolution was reached in 2013, and researchers &quot;can now routinely produce three-dimensional structures of biomolecules,&quot; according to the Nobel committee.&nbsp;

The trio will share the prize money of nine million Swedish kronor (around $1.1 million or 943,100 euros).

&quot;Normally what I&#39;d do if I was in Cambridge, we will have a party around tea-time in the lab but I expect we&#39;ll have it tomorrow instead,&quot; said Henderson.

&#39;Beautiful pictures&#39;&nbsp;

The prize announcement was praised by the scientific community and observers around the world.

&quot;By solving more and more structures at the atomic level we can answer biological questions, such as how drugs get into cells, that were simply unanswerable a few years ago,&quot; Jim Smith, science director at the London-based biomedical research charity Wellcome, said in a statement.&nbsp;

Daniel Davis, immunology professor at the University of Manchester, said details of crucial molecules and proteins that make the human immune system function, can now be seen like never before.

&quot;It has been used in visualising the way in which antibodies can work to stop viruses being dangerous, leading to new ideas for medicines &ndash;- as just one example,&quot; he said.&nbsp;

John Hardy, neuroscience professor at University College London, said Dubochet, Frank and Henderson&#39;s technique has transformed the field of structural biology.

It has been used, for example, to compile a detailed identikit of an enzyme implicated in Alzheimer&#39;s.

&quot;Knowing this structure opens up the possibility of rational drug design in this area,&quot; Hardy said.&nbsp;&nbsp;

&quot;And as a biologist, I can say that the pictures are beautiful.&quot;

The trio won for the development of cryo-electron microscopy, a method of simplifying and improving the imaging of biomolecules

A revolutionary technique dubbed cryo-electron microscopy, which has shed light on the Zika virus and an Alzheimer's enzyme earned scientists Jacques Dubochet, Joachim Frank and Richard Henderson the Nobel Chemistry Prize on Wednesday. Thanks to the international team's "cool method", which uses electron beams to examine the tiniest structures of cells, "researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen," the Nobel chemistry committee said. This has been "decisive for both the basic understanding of life's chemistry and for the development of pharmaceuticals," it added. The ultra-sensitive imaging method allows molecules to be flash-frozen and studied in their natural form, without the need for dyes. It has laid bare never-before-seen details of the tiny protein machines that run all cells. "When researchers began to suspect that the Zika virus was causing the epidemic of brain-damaged newborns in Brazil, they turned to cryo-EM (electron microscopy) to visualise the virus," the committee said. Frank, a 77-year-old, German-born biochemistry professor at Columbia University in New York, was woken from his sleep when the committee announced the prize in Stockholm, six hours ahead. "There are so many other discoveries every day, I was in a way speechless," he said. "It's wonderful news." In the first half of the 20th century, biomolecule, proteins, DNA and RNA, were terra incognita on the map of biochemistry. Because the powerful electron beam destroys biological material, electron microscopes were long thought to be useful only to study the dead matter. Tea party to celebrate But 72-year-old Henderson, from the MRC Laboratory of Molecular Biology in Cambridge, used an electron microscope in 1990 to generate a three-dimensional image of a protein at atomic resolution, a groundbreaking discovery which proved the technology's potential. Frank made it widely usable between 1975 and 1986, developing a method to transform the electron microscope's fuzzy two-dimensional images into sharp, 3-D composites. Dubochet, today an honorary professor of biophysics at the University of Lausanne, added water. Now 75, he discovered in the 1980s how to cool water so quickly that it solidifies in liquid form around a biological sample, allowing the molecules to retain their natural shape even in a vacuum. The electron microscope's every nut and bolt have been optimised since these discoveries. The required atomic resolution was reached in 2013, and researchers "can now routinely produce three-dimensional structures of biomolecules," according to the Nobel committee. The trio will share the prize money of nine million Swedish kronor (around $1.1 million or 943,100 euros). "Normally what I'd do if I was in Cambridge, we will have a party around tea-time in the lab but I expect we'll have it tomorrow instead," said Henderson. 'Beautiful pictures' The prize announcement was praised by the scientific community and observers around the world. "By solving more and more structures at the atomic level we can answer biological questions, such as how drugs get into cells, that were simply unanswerable a few years ago," Jim Smith, science director at the London-based biomedical research charity Wellcome, said in a statement. Daniel Davis, immunology professor at the University of Manchester, said details of crucial molecules and proteins that make the human immune system function, can now be seen like never before. "It has been used in visualising the way in which antibodies can work to stop viruses being dangerous, leading to new ideas for medicines –- as just one example," he said. John Hardy, neuroscience professor at University College London, said Dubochet, Frank and Henderson's technique has transformed the field of structural biology. It has been used, for example, to compile a detailed identikit of an enzyme implicated in Alzheimer's. "Knowing this structure opens up the possibility of rational drug design in this area," Hardy said. "And as a biologist, I can say that the pictures are beautiful."

Chemistry Nobel awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson

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Scientists Jacques Dubochet, Joachim Frank, Richard Henderson share 2017 Nobel Prize in chemistry

Chemistry Nobel awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson