Researchers can measure distances in molecules optically

A team led by physicists Steffen Sahl and Stefan Hell at the Max Planck Institute for Multidisciplinary Sciences in Göttingen and the Max Planck Institute for Medical Research in Heidelberg has succeeded in measuring distances within biomolecules using a light microscope, down to one nanometer and with Ångström precision. The intra-molecular resolution achieved with MINFLUX microscopy makes it possible to optically record the spatial distances between subunits in macromolecules and thus to detect different conformations of individual proteins in the light microscope.  

Polyprolines of different lengths, relatively stiff polypeptides, served as intramolecular “nanometer rulers” to demonstrate the highest MINFLUX resolutions in the Förster resonance energy transfer (FRET) distance range. The 2-sigma ellipses show the measurement uncertainty of the individual positions.

What does it look like in the nanocosmos of living cells? Fluorescence microscopy makes it possible to visualize specific molecules in cells or tissues and has become an integral part of biological and basic medical research. With the help of new high-resolution fluorescence nanoscopy concepts such as MINFLUX microscopy, even closely spaced biomolecules can be separated from each other using a light microscope. Accurately imaging the inside of cells is one thing, but can fluorescence microscopy also be used to measure details within individual proteins or other macromolecules?

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