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Diffraction-unlimited all-optical imaging and writing with a photochromic GFP

Author

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  • Tim Grotjohann

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Ilaria Testa

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Marcel Leutenegger

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Hannes Bock

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Nicolai T. Urban

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Flavie Lavoie-Cardinal

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Katrin I. Willig

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Christian Eggeling

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Stefan Jakobs

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
    University of Göttingen Medical School, Robert-Koch-Str. 40, 37075 Göttingen, Germany)

  • Stefan W. Hell

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

Abstract

Lens-based optical microscopy failed to discern fluorescent features closer than 200 nm for decades, but the recent breaking of the diffraction resolution barrier by sequentially switching the fluorescence capability of adjacent features on and off is making nanoscale imaging routine. Reported fluorescence nanoscopy variants switch these features either with intense beams at defined positions or randomly, molecule by molecule. Here we demonstrate an optical nanoscopy that records raw data images from living cells and tissues with low levels of light. This advance has been facilitated by the generation of reversibly switchable enhanced green fluorescent protein (rsEGFP), a fluorescent protein that can be reversibly photoswitched more than a thousand times. Distributions of functional rsEGFP-fusion proteins in living bacteria and mammalian cells are imaged at

Suggested Citation

  • Tim Grotjohann & Ilaria Testa & Marcel Leutenegger & Hannes Bock & Nicolai T. Urban & Flavie Lavoie-Cardinal & Katrin I. Willig & Christian Eggeling & Stefan Jakobs & Stefan W. Hell, 2011. "Diffraction-unlimited all-optical imaging and writing with a photochromic GFP," Nature, Nature, vol. 478(7368), pages 204-208, October.
  • Handle: RePEc:nat:nature:v:478:y:2011:i:7368:d:10.1038_nature10497
    DOI: 10.1038/nature10497
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    Cited by:

    1. Yueli Yang & Xueyang Bai & Fanghao Hu, 2024. "Photoswitchable polyynes for multiplexed stimulated Raman scattering microscopy with reversible light control," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Hui-Wen Lu-Walther & Wenya Hou & Martin Kielhorn & Yoshiyuki Arai & Takeharu Nagai & Michael M Kessels & Britta Qualmann & Rainer Heintzmann, 2016. "Nonlinear Structured Illumination Using a Fluorescent Protein Activating at the Readout Wavelength," PLOS ONE, Public Library of Science, vol. 11(10), pages 1-14, October.

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