For the first time, a single atom was observed in a frozen electric mirror

electroscope map of ferringin. Photo Source: Paul Emsley/MRC Laboratory of Molecular Biology
Frozen Electroscope produces the clearest image yet and identifies a single atom in a protein for the first time. The breakthrough, reported by two laboratories at the end of May, cemented the status of frozen electroscopes as the primary tool for mapping protein 3D shapes, Nature reported.
"It's a milestone, that's for sure. There really is nothing to break through, this is the final resolution barrier. Holger Stark, a biochemist and electron microscope at the Max Planck Institute for Biophysical Chemistry in Germany who led one of the studies, said. Another study was led by Sjors Scheres and Radu Ariescu, structural biologists at the Molecular Biology Laboratory of the Cambridge Medical Research Council. Both articles were published on the bioRxiv preprint server.
atomic resolution map is accurate enough to clearly distinguish the position of individual atoms in a protein at a resolution of about 1.2×10
meters. These structures are particularly useful for understanding how enzymes work and using these insights to identify drugs that block their activity.
to get the frozen electroscope to atomic resolution, the two teams studied a protein called ferrine. Because of its stability, the protein has become a test bench for cryo-electric mirrors: the protein structure has a resolution of 1.54×10
meters, which was previously recorded.
, the team improved their techniques to take clearer photos of ferringin. Stark's team obtained a 1.25×10-
structure of the protein, improving the resolution of the resulting image.
1.2×10
m structure obtained by the British team is very complete, Scheres said, they can distinguish between proteins and individual hydrogen atoms in surrounding water molecules×
Scheres and Arcescu have also tested improvements to a simplified form of protein called GABAA receptors. Located in the neuron membrane, this protein is a target for general anaesthetic, anxiety drugs and many other drugs. Last year, the Aricescu team used a frozen electroscope to position the protein at 2.5 × 10
meters. But using the new kit, the researchers obtained a resolution of 1.7×10
meters. "It's like peeling a blur off your eyes," Aricescu said. At this resolution, a complete universe × 10
0.5 to 10 meters. Scheres
, said the breakthroughs could cement the position of cryoscopes as the tool of choice for most structural studies. But Stark believes X-ray crystallology retains some appeal. If a protein can crystallize, it can produce structures that combine with thousands of potential drugs relatively efficiently in a very short period of time, but it still takes hours to days to generate enough data for very high-resolution cryogenic electromagnetic structures.
each technology has its advantages and disadvantages," says Stark, a research expert. Many papers and comments have been published that these latest advances in cryoscopic electroscopes will be x-ray death signals. I doubt it. Information
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