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Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study

Hellenkamp, Björn, Schmid, Sonja, Doroshenko, Olga, Opanasyuk, Oleg, Kühnemuth, Ralf, Rezaei Adariani, Soheila, Ambrose, Benjamin, Aznauryan, Mikayel, Barth, Anders, Birkedal, Victoria, Bowen, Mark E., Chen, Hongtao, Cordes, Thorben, Eilert, Tobias, Fijen, Carel, Gebhardt, Christian, Götz, Markus, Gouridis, Giorgos, Gratton, Enrico, Ha, Taekjip, Hao, Pengyu, Hanke, Christian A., Hartmann, Andreas, Hendrix, Jelle, Hildebrandt, Lasse L., Hirschfeld, Verena, Hohlbein, Johannes, Hua, Boyang, Hübner, Christian G., Kallis, Eleni, Kapanidis, Achillefs N., Kim, Jae-Yeol, Krainer, Georg, Lamb, Don C., Lee, Nam Ki, Lemke, Edward A., Levesque, Brié, Levitus, Marcia, McCann, James J., Naredi-Rainer, Nikolaus, Nettels, Daniel, Ngo, Thuy, Qiu, Ruoyi, Robb, Nicole C., Röcker, Carlheinz, Sanabria, Hugo, Schlierf, Michael, Schröder, Tim, Schuler, Benjamin, Seidel, Henning, Streit, Lisa, Thurn, Johann, Tinnefeld, Philip, Tyagi, Swati, Vandenberk, Niels, Vera, Andrés Manuel, Weninger, Keith R., Wünsch, Bettina, Yanez-Orozco, Inna S., Michaelis, Jens, Seidel, Claus A. M., Craggs, Timothy D., Hugel, Thorsten·2018·Nature Methods
DOI 10.1038/s41592-018-0085-0PMC PMC6121742
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  • The combination of array tomography with FRET enhances the lateral resolution to ~10 nm in the selected single synaptic terminals allowing us to determine whether proteins are close enough to be interacting.

    “The combination of array tomography with FRET enhances the lateral resolution to ~ 10 nm in the selected single synaptic terminals allowing us to determine whether proteins are close enough to be interacting [23, 52].”

    From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [23]

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Research works printed but not linked: 51

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Metadata

Authors
Hellenkamp, B., Schmid, S., Doroshenko, O., Opanasyuk, O., Kühnemuth, R., Rezaei Adariani, S., Ambrose, B., Aznauryan, M., Barth, A., Birkedal, V., Bowen, M. E., Chen, H., Cordes, T., Eilert, T., Fijen, C., Gebhardt, C., Götz, M., Gouridis, G., Gratton, E., Ha, T., Hao, P., Hanke, C. A., Hartmann, A., Hendrix, J., Hildebrandt, L. L., Hirschfeld, V., Hohlbein, J., Hua, B., Hübner, C. G., Kallis, E., Kapanidis, A. N., Kim, J.-Y., Krainer, G., Lamb, D. C., Lee, N. K., Lemke, E. A., Levesque, B., Levitus, M., McCann, J. J., Naredi-Rainer, N., Nettels, D., Ngo, T., Qiu, R., Robb, N. C., Röcker, C., Sanabria, H., Schlierf, M., Schröder, T., Schuler, B., Seidel, H., Streit, L., Thurn, J., Tinnefeld, P., Tyagi, S., Vandenberk, N., Vera, A. M., Weninger, K. R., Wünsch, B., Yanez-Orozco, I. S., Michaelis, J., Seidel, C. A. M., Craggs, T. D., & Hugel, T.
ORCID
Venue
Nature Methods
Publisher
Springer Science and Business Media LLC
Published
2018-08-31
Volume
15
Issue
9
Pages
669-676
ISSN
  • 1548-7091
  • 1548-7105
DOI
10.1038/s41592-018-0085-0
PMC
PMC6121742
Cited by
519
References
0
Language
en
Update notices
correction (2018-10-16)
Licence
creativecommons.org/licenses/by/4.0 (tdm)

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