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Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography
Cellini, A., Shankar, M. K., Nimmrich, A., Hunt, L. A., Monrroy, L., Mutisya, J., … Westenhoff, S. (2024). Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography. Nature Chemistry. https://doi.org/10.1038/s41557-023-01413-9
Low-pass spectral analysis of time-resolved serial femtosecond crystallography data
Casadei, C. M., Hosseinizadeh, A., Bliven, S., Weinert, T., Standfuss, J., Fung, R., … Santra, R. (2023). Low-pass spectral analysis of time-resolved serial femtosecond crystallography data. Structural Dynamics, 10(3), 034101 (18 pp.). https://doi.org/10.1063/4.0000178
Ultrafast structural changes direct the first molecular events of vision
Gruhl, T., Weinert, T., Rodrigues, M. J., Milne, C. J., Ortolani, G., Nass, K., … Panneels, V. (2023). Ultrafast structural changes direct the first molecular events of vision. Nature, 615, 939-944. https://doi.org/10.1038/s41586-023-05863-6
Kilohertz serial crystallography with the JUNGFRAU detector at a fourth-generation synchrotron source
Leonarski, F., Nan, J., Matej, Z., Bertrand, Q., Furrer, A., Gorgisyan, I., … Dworkowski, F. (2023). Kilohertz serial crystallography with the JUNGFRAU detector at a fourth-generation synchrotron source. IUCrJ, 10(6), 729-737. https://doi.org/10.1107/S2052252523008618
Visualizing the DNA repair process by a photolyase at atomic resolution
Maestre-Reyna, M., Wang, P. H., Nango, E., Hosokawa, Y., Saft, M., Furrer, A., … Tsai, M. D. (2023). Visualizing the DNA repair process by a photolyase at atomic resolution. Science, 382(6674), eadd7795 (14 pp.). https://doi.org/10.1126/science.add7795
A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers
Wranik, M., Kepa, M. W., Beale, E. V., James, D., Bertrand, Q., Weinert, T., … Standfuss, J. (2023). A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers. Nature Communications, 14(1), 7956 (12 pp.). https://doi.org/10.1038/s41467-023-43523-5
Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography
Wranik, M., Weinert, T., Slavov, C., Masini, T., Furrer, A., Gaillard, N., … Standfuss, J. (2023). Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography. Nature Communications, 14(1), 903 (12 pp.). https://doi.org/10.1038/s41467-023-36481-5
Structural basis of the radical pair state in photolyases and cryptochromes
Cellini, A., Shankar, M. K., Wahlgren, W. Y., Nimmrich, A., Furrer, A., James, D., … Westenhoff, S. (2022). Structural basis of the radical pair state in photolyases and cryptochromes. Chemical Communications, 58(31), 4889-4892. https://doi.org/10.1039/D2CC00376G
<em>In vivo</em> photocontrol of microtubule dynamics and integrity, migration and mitosis, by the potent GFP-imaging-compatible photoswitchable reagents SBTubA4P and SBTub2M
Gao, L., Meiring, J. C. M., Varady, A., Ruider, I. E., Heise, C., Wranik, M., … Thorn-Seshold, O. (2022). In vivo photocontrol of microtubule dynamics and integrity, migration and mitosis, by the potent GFP-imaging-compatible photoswitchable reagents SBTubA4P and SBTub2M. Journal of the American Chemical Society, 144(12), 5614-5628. https://doi.org/10.1021/jacs.2c01020
Acoustic levitation and rotation of thin films and their application for room temperature protein crystallography
Kepa, M. W., Tomizaki, T., Sato, Y., Ozerov, D., Sekiguchi, H., Yasuda, N., … Tsujino, S. (2022). Acoustic levitation and rotation of thin films and their application for room temperature protein crystallography. Scientific Reports, 12, 5349 (14 pp.). https://doi.org/10.1038/s41598-022-09167-z
Dynamics and mechanism of a light-driven chloride pump
Mous, S., Gotthard, G., Ehrenberg, D., Sen, S., Weinert, T., Johnson, P. J. M., … Nogly, P. (2022). Dynamics and mechanism of a light-driven chloride pump. Science, 375(6583), 845-851. https://doi.org/10.1126/science.abj6663
Crystallization systems for the high-resolution structural analysis of tubulin-ligand complexes
Mühlethaler, T., Olieric, N., Ehrhard, V. A., Wranik, M., Standfuss, J., Sharma, A., … Steinmetz, M. O. (2022). Crystallization systems for the high-resolution structural analysis of tubulin-ligand complexes. In H. Inaba (Ed.), Methods in molecular biology: Vol. 2430. Microtubules. Methods and protocols (pp. 349-374). https://doi.org/10.1007/978-1-0716-1983-4_23
A robust, GFP-orthogonal photoswitchable inhibitor scaffold extends optical control over the microtubule cytoskeleton
Gao, L., Meiring, J. C. M., Kraus, Y., Wranik, M., Weinert, T., Pritzl, S. D., … Thorn-Seshold, O. (2021). A robust, GFP-orthogonal photoswitchable inhibitor scaffold extends optical control over the microtubule cytoskeleton. Cell Chemical Biology, 28(2), 228-241. https://doi.org/10.1016/j.chembiol.2020.11.007
Pink-beam serial femtosecond crystallography for accurate structure-factor determination at an X-ray free-electron laser
Nass, K., Bacellar, C., Cirelli, C., Dworkowski, F., Gevorkov, Y., James, D., … Milne, C. J. (2021). Pink-beam serial femtosecond crystallography for accurate structure-factor determination at an X-ray free-electron laser. IUCrJ, 8, 905-920. https://doi.org/10.1107/S2052252521008046
Advances in long-wavelength native phasing at X-ray free-electron lasers
Nass, K., Cheng, R., Vera, L., Mozzanica, A., Redford, S., Ozerov, D., … Milne, C. J. (2020). Advances in long-wavelength native phasing at X-ray free-electron lasers. IUCrJ, 7, 965-975. https://doi.org/10.1107/S2052252520011379
Femtosecond-to-millisecond structural changes in a light-driven sodium pump
Skopintsev, P., Ehrenberg, D., Weinert, T., James, D., Kar, R. K., Johnson, P. J. M., … Standfuss, J. (2020). Femtosecond-to-millisecond structural changes in a light-driven sodium pump. Nature, 583, 314-318. https://doi.org/10.1038/s41586-020-2307-8
A tool for visualizing protein motions in time-resolved crystallography
Wickstrand, C., Katona, G., Nakane, T., Nogly, P., Standfuss, J., Nango, E., & Neutze, R. (2020). A tool for visualizing protein motions in time-resolved crystallography. Structural Dynamics, 7, 024701 (12 pp.). https://doi.org/10.1063/1.5126921
Arrestin-1 engineering facilitates complex stabilization with native rhodopsin
Haider, R. S., Wilhelm, F., Rizk, A., Mutt, E., Deupi, X., Peterhans, C., … Ostermaier, M. K. (2019). Arrestin-1 engineering facilitates complex stabilization with native rhodopsin. Scientific Reports, 9(1), 439 (13 pp.). https://doi.org/10.1038/s41598-018-36881-4
Structural basis for allosteric ligand recognition in the human CC chemokine receptor 7
Jaeger, K., Bruenle, S., Weinert, T., Guba, W., Muehle, J., Miyazaki, T., … Standfuss, J. (2019). Structural basis for allosteric ligand recognition in the human CC chemokine receptor 7. Cell, 178(5), 1222-1230. https://doi.org/10.1016/j.cell.2019.07.028
Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
Mayer, D., Damberger, F. F., Samarasimhareddy, M., Feldmueller, M., Vuckovic, Z., Flock, T., … Veprintsev, D. B. (2019). Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation. Nature Communications, 10, 1261 (14 pp.). https://doi.org/10.1038/s41467-019-09204-y