Cryo-electron Microscopy Technology Helps Make New Strides In Biomolecular Imaging

Biomolecular imaging has always been essential to the field of biochemistry. Without knowing the structure of biomolecules, we wouldn't have understood how enzymes work in our bodies to catalyze reactions that would otherwise react at a snail's pace. In conclusion,the ability to find the structure of biomolecules helps us carve out the scientific way how life goes on day by day.

Biomolecular imaging has been improving through the years. However, a new technology called Cryo-Electron Microscopy gives a more detailed image and as a result helps us understand the properties of a molecule even better. In short, it will revolutionize the way scientists look at biomolecules from now on. For example, the image below clearly shows the magnitude of the difference in resolution between the microscopic image of a biomolecule by using older technology versus using the newer technology.

(Courtesy to Royal Swedish Academy of Sciences)

This ingenious technology was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson who all won the Nobel Prize for Chemistry this year for developing this. The research and development for this began way before the 2000's and is divided precisely into three parts with each part corresponding to each scientist.

In the 1990's, Richard Henderson succeeded in developing an electron microscope that can capture the structure of biomolecules in atomic resolution. For Dubochet's work, I would recommend that you follow with the explanation while looking at the figure provided below this paragraph for better understanding. In the 1980's, Jacques Dubochet found a way to prevent the biomolecule from disappearing as a result of the water evaporating because of the vacuum created by the electron microscope. He accomplished this by transferring the sample onto a micro-mesh that filters out excess matter. Then, the sample forms a thin film across the holes of the micro-mesh and that is shot into Ethane at -196 degrees celsius. As a result, the water cools very rapidly and "freezes" around the sample which is then cooled by liquid nitrogen when measurements are taken by the electron microscope. This, as a result, helps retain the shape of the biomolecule which allows for more detailed analysis of its structure.

(Courtesy to The Royal Swedish Academy of Sciences)

Again I would recommend that you follow this explanation with the figure provided below for better understanding of Frank's image processing proedure.Last but not the least, during the 70's and 80's Joachim Frank found a way to compile the low resolution 2-dimensional images of the biomolecules and generate a high resolution 3-dimensional image of the molecule. Firstly, randomly oriented proteins are scanned by an electron beam which leaves a trace. The computer then analyzes these traces and the backgrounds created and decides to place similar looking ones in a group. Then the computer uses countless other traces to generate high resolution 2-dimensional images which are then compiled into a 3-dimensional image by the computer.

(Courtesy to Royal Swedish Academy Of Sciences)

The true potential of this technology is unimaginable in that it is huge.For example, it is possible that we can better understand how viruses interact with our bodies which could help us produce more effective antidotes. In addition to saving lives, it can also inflate the bank of knowledge that we already possess about the biomolecular processes that are keeping us alive day to day.

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