Cryo-electron microscopy, which has made countless scientists successful, finally won the 2017 Nobel Prize in Chemistry!
Thread Content
At 5:45 pm on October 4, Beijing time, the Nobel Prize Committee announced that the 2017 Nobel Prize in Chemistry will be awarded to Jacques Dubochet of Switzerland, Joachim Frank of the United States, and Richard Henderson of the United Kingdom in recognition of their outstanding contributions to cryo-electron microscopy technology.
The following is the official press release of the Nobel Committee: We may soon be able to obtain atomic-level resolution pictures of the complex mechanisms of life. This is why the 2017 Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for their outstanding contributions to cryo-electron microscopy, which simplified cryo-electron microscopy and applied it to biomolecule imaging. This imaging technology has propelled the field of biochemistry into a new era. Seeing is believing, and imaging technology holds the key to understanding the truth. Many major scientific advances are based on classic imaging technologies, which can truly present items invisible to our naked eyes to scientists. However, the road to biochemical research is full of difficulties, and many studies have been blank so far because there are few effective imaging technologies that can be applied to molecular-level mechanisms in biology. However, cryo-electron microscopy will change that. Thanks to this, researchers can now freeze moving biomolecules and then use cryo-electron microscopy to image them, revealing processes that we could not observe before. Such technology will be very beneficial to our understanding of the field of life science chemistry and drug research.
Electron microscopy technology has been around for a long time and is suitable for "inanimate" samples. However, because it emits destructive electron beams, it is not suitable for the study of biological materials and biomolecules. However, in 1990, Richard Henderson used electron microscopy to successfully image the three-dimensional structure of proteins at atomic-level resolution. Such progress also proved the potential of electron microscopy. From 1975 to 1986, Joachim Frank invented an image processing method that could use electron microscopes to analyze blurry two-dimensional images and present them in the form of three-dimensional structures. Jacques Dubochet made it possible to observe water-containing samples using electron microscopy. Generally speaking, electron microscopes need to work in a vacuum environment, and the water in the sample needs to be evaporated, thereby destroying the biomolecules in the sample. Therefore, in the 1980s, Dubochet succeeded in rapidly cooling the aqueous solution environment into a glassy state, freezing the surrounding biomolecules so that the biomolecules could maintain their natural structural state for easy observation with a microscope.
Based on the findings above, every component on the electron microscope has been optimized. In 2013, it became possible to resolve the three-dimensional structure of biomolecules at the atomic level. In recent years, using cryo-electron microscopy technology, we often see images of protein molecules and the surface of Zika viruses in some literature. Biochemistry is facing explosive developments, and what an exciting future it all has.
See the microscopic world more clearly
It is more possible to study the microscopic world. In fact, it is currently used more in biotechnology.
It’s also a big benefit to the medical field, right?