Direct optical measurement of intramolecular distances with angstrom precision
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| Název: | Direct optical measurement of intramolecular distances with angstrom precision |
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| Autoři: | Steffen J. Sahl, Jessica Matthias, Kaushik Inamdar, Michael Weber, Taukeer A. Khan, Christian Brüser, Stefan Jakobs, Stefan Becker, Christian Griesinger, Johannes Broichhagen, Stefan W. Hell |
| Přispěvatelé: | Sahl, Steffen J., Matthias, Jessica, Inamdar, Kaushik, Weber, Michael, Khan, Taukeer A., Brüser, Christian, Jakobs, Stefan, Becker, Stefan, Griesinger, Christian, Broichhagen, Johannes, Hell, Stefan W. |
| Zdroj: | Science |
| Informace o vydavateli: | American Association for the Advancement of Science (AAAS), 2024. |
| Rok vydání: | 2024 |
| Témata: | Protein Subunits, Histidine Kinase, Microscopy, Fluorescence, Protein Domains, Fluorescence Resonance Energy Transfer, Humans, Proteins, Protein Multimerization, Peptides |
| Popis: | Optical investigations of nanometer distances between proteins, their subunits, or other biomolecules have been the exclusive prerogative of Förster resonance energy transfer (FRET) microscopy for decades. In this work, we show that MINFLUX fluorescence nanoscopy measures intramolecular distances down to 1 nanometer—and in planar projections down to 1 angstrom—directly, linearly, and with angstrom precision. Our method was validated by quantifying well-characterized 1- to 10-nanometer distances in polypeptides and proteins. Moreover, we visualized the orientations of immunoglobulin subunits, applied the method in human cells, and revealed specific configurations of a histidine kinase PAS domain dimer. Our results open the door for examining proximities and interactions by direct position measurements at the intramacromolecular scale. |
| Druh dokumentu: | Article |
| Jazyk: | English |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.adj7368 |
| Přístupová URL adresa: | https://pubmed.ncbi.nlm.nih.gov/39388556 https://resolver.sub.uni-goettingen.de/purl?gro-2/146352 |
| Přístupové číslo: | edsair.doi.dedup.....eaea790b0fc4907618255e329d3ac559 |
| Databáze: | OpenAIRE |
Nájsť tento článok vo Web of Science | Abstrakt: | Optical investigations of nanometer distances between proteins, their subunits, or other biomolecules have been the exclusive prerogative of Förster resonance energy transfer (FRET) microscopy for decades. In this work, we show that MINFLUX fluorescence nanoscopy measures intramolecular distances down to 1 nanometer—and in planar projections down to 1 angstrom—directly, linearly, and with angstrom precision. Our method was validated by quantifying well-characterized 1- to 10-nanometer distances in polypeptides and proteins. Moreover, we visualized the orientations of immunoglobulin subunits, applied the method in human cells, and revealed specific configurations of a histidine kinase PAS domain dimer. Our results open the door for examining proximities and interactions by direct position measurements at the intramacromolecular scale. |
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| ISSN: | 10959203 00368075 |
| DOI: | 10.1126/science.adj7368 |