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High resolution electron microscope inaugurated at the University of Cologne

The Institute of Biochemistry has installed a new Titan Krios electron microscope with a resolution so high that it allows scientists to watch proteins at work.

The new Titan Krios electron microscope has been put into operation at the Faculty of Mathematics and Natural Sciences. In 2017, the University of Cologne obtained a large-scale equipment grant of 5 million euros from the German Research Foundation (DFG) to launch a central platform for molecular cryo-EM StruBiTEM (structural biology cryo-transmission electron microscopy). At the heart of this platform is the Titan Krios electron microscope, now in operation, which allows scientists to observe proteins, the active building blocks of our cells, at work. The state-of-the-art instrument makes it possible to study even tiny proteins down to the atomic level. The molecular structure of these proteins can be revealed at a resolution of better than 2 angstroms, allowing  one to see the hole in an aromatic ring.

‘We can use this technique to look at proteins in their natural environment and determine where which amino acid sits in the protein, and thus determine their functional role,’ said scientific director of StrubiTEM Professor Dr Elmar Behrmann of the Institute of Biochemistry.

The method’s diverse contributions range from discoveries in basic research to applications in clinical research. Specifically, these include current research on COVID-19 structures that have already been solved by this technology.

‘Among other things, establishing the method at the Faculty of Mathematics and Natural Sciences has the potential of building bridges between basic research and medical research in Cologne,’ Behrmann added. He also noted that the new technology has been met with great interest among researchers in Cologne: ‘We have already established collaborations with major research projects in Cologne and look forward to working together.’

In cryo-electron microscopy, samples, especially isolated proteins, but also viruses or polymers, are frozen at high speed within milliseconds. This prevents ice crystals from forming, which would destroy the structure of the proteins. This ensures that the samples viewed in the microscope correspond exactly to their state in solution – even time-resolved studies are possible to view a protein at different stages of its activity.

For freezing, the scientists use liquid-nitrogen cooled ethane: ‘We freeze so fast that the water does not have time to form crystals – within milliseconds,’ Behrmann remarked. ‘This corresponds to the time scale on which important structural changes take place in proteins. So we can be sure that they remain unaltered in their initial state.’

Media Contact:
Professor Dr. Elmar Behrmann
Institute of Biochemistry, University of Cologne
+49 221 470 76300

Press and Communications Team:
Robert Hahn
+49 221 470 2396

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