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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
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
<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
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
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
Improving high viscosity extrusion of microcrystals for time-resolved serial femtosecond crystallography at X-ray lasers
James, D., Weinert, T., Skopintsev, P., Furrer, A., Gashi, D., Tanaka, T., … Standfuss, J. (2019). Improving high viscosity extrusion of microcrystals for time-resolved serial femtosecond crystallography at X-ray lasers. Journal of Visualized Experiments, 2019(144), e59087 (12 pp.). https://doi.org/10.3791/59087
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
Membrane protein dynamics studied by X-ray lasers - or why only time will tell
Standfuss, J. (2019). Membrane protein dynamics studied by X-ray lasers - or why only time will tell. Current Opinion in Structural Biology, 57, 63-71. https://doi.org/10.1016/j.sbi.2019.02.001
Bacteriorhodopsin: structural insights revealed using X-ray lasers and synchrotron radiation
Wickstrand, C., Nogly, P., Nango, E., Iwata, S., Standfuss, J., & Neutze, R. (2019). Bacteriorhodopsin: structural insights revealed using X-ray lasers and synchrotron radiation. Annual Review of Biochemistry, 88, 59-83. https://doi.org/10.1146/annurev-biochem-013118-111327
Ligand channel in pharmacologically stabilized rhodopsin
Mattle, D., Kuhn, B., Aebi, J., Bedoucha, M., Kekilli, D., Grozinger, N., … Dawson, R. J. P. (2018). Ligand channel in pharmacologically stabilized rhodopsin. Proceedings of the National Academy of Sciences of the United States of America PNAS, 115(14), 3640-3645. https://doi.org/10.1073/pnas.1718084115
Crystal structure of rhodopsin in complex with a mini-G<sub>o</sub> sheds light on the principles of G protein selectivity
Tsai, C. J., Pamula, F., Nehmé, R., Mühle, J., Weinert, T., Flock, T., … Schertler, G. F. X. (2018). Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of G protein selectivity. Science Advances, 4(9), aat7052 (9 pp.). https://doi.org/10.1126/sciadv.aat7052
Perspective: opportunities for ultrafast science at SwissFEL
Abela, R., Beaud, P., van Bokhoven, J. A., Chergui, M., Feurer, T., Haase, J., … Patthey, L. (2017). Perspective: opportunities for ultrafast science at SwissFEL. Structural Dynamics, 4(6), 61602 (25 pp.). https://doi.org/10.1063/1.4997222
Serial crystallography at synchrotrons and X-ray lasers
Standfuss, J., & Spence, J. (2017). Serial crystallography at synchrotrons and X-ray lasers. IUCrJ, 4, 100-101. https://doi.org/10.1107/S2052252517001877
Structural biology: signalling under the microscope
Tsai, C. J., & Standfuss, J. (2017). Structural biology: signalling under the microscope. Nature, 546(7656), 36-37. https://doi.org/10.1038/nature22491
A three-dimensional movie of structural changes in bacteriorhodopsin
Nango, E., Royant, A., Kubo, M., Nakane, T., Wickstrand, C., Kimura, T., … Iwata, S. (2016). A three-dimensional movie of structural changes in bacteriorhodopsin. Science, 354(6319), 1552-1557. https://doi.org/10.1126/science.aaH3497
Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography
Nogly, P., Panneels, V., Nelson, G., Gati, C., Kimura, T., Milne, C., … Standfuss, J. (2016). Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography. Nature Communications, 7, 12314 (9 pp.). https://doi.org/10.1038/ncomms12314
Functional map of arrestin binding to phosphorylated opsin, with and without agonist
Peterhans, C., Lally, C. C. M., Ostermaier, M. K., Sommer, M. E., & Standfuss, J. (2016). Functional map of arrestin binding to phosphorylated opsin, with and without agonist. Scientific Reports, 6, 28686 (14 pp.). https://doi.org/10.1038/srep28686