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Biological molecules can be observed at the nanoscale with fluorescence nanoscopy. Researchers at IRIG develop this technique at cryogenic temperature. To this aim, they study how fluorescent proteins markers behave at very cold temperatures. They deciphered how the fluorescent protein rsEGFP2 works under cryogenic conditions. They devised an upgraded cryo-microscope that they now aim to make available to the scientific community.
Single-molecule localization microscopy (SMLM) improves the resolution of fluorescence microscopy normally limited by diffraction. One challenge is to work at cryogenic temperature to preserve the native structure of the investigated samples, like in cryo electron microscopy. The “magic” of SMLM lies in the properties of the employed fluorophores used to label the biological target. Those fluorophores are able to efficiently switch between a fluorescent on-state and a nonfluorescent off-state. However photoswitching is killed at very low temperature.
Mantovanelli A M R, Glushonkov O, Adam V, Wulffelé J, Thédié D, Byrdin M, Gregor I, Nevskyi O, Enderlein J and Bourgeois DPhotophysical Studies at Cryogenic Temperature Reveal a Novel Photoswitching Mechanism of rsEGFP2
Journal of the American Chemical Society 2023
CEA is a French government-funded technological research organisation in four main areas: low-carbon energies, defense and security, information technologies and health technologies. A prominent player in the European Research Area, it is involved in setting up collaborative projects with many partners around the world.