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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
Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from <em>Selenomonas ruminantium</em> provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family
Bertrand, Q., Coquille, S., Iorio, A., Sterpone, F., & Madern, D. (2023). Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases. Journal of Structural Biology, 215(4), 108039 (13 pp.). https://doi.org/10.1016/j.jsb.2023.108039
Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs
Carrillo, M., Mason, T. J., Karpik, A., Martiel, I., Kepa, M. W., McAuley, K. E., … Padeste, C. (2023). Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs. IUCrJ, 10(6), 678-693. https://doi.org/10.1107/S2052252523007595
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
Time-resolved crystallography captures light-driven DNA repair
Christou, N. E., Apostolopoulou, V., Melo, D. V. M., Ruppert, M., Fadini, A., Henkel, A., … Lane, T. J. (2023). Time-resolved crystallography captures light-driven DNA repair. Science, 382(6674), 1015-1020. https://doi.org/10.1126/science.adj4270
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
Deciphering evolutionary trajectories of lactate dehydrogenases provides new insights into allostery
Robin, A. Y., Brochier-Armanet, C., Bertrand, Q., Barette, C., Girard, E., & Madern, D. (2023). Deciphering evolutionary trajectories of lactate dehydrogenases provides new insights into allostery. Molecular Biology and Evolution, 40(10), msad223 (22 pp.). https://doi.org/10.1093/molbev/msad223
Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect
Rodrigues, M. J., Casadei, C. M., Weinert, T., Panneels, V., & Schertler, G. F. X. (2023). Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect. Acta Crystallographica Section D: Structural Biology, 79(3), D79 (10 pp.). https://doi.org/10.1107/S2059798323000931
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
Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre
Båth, P., Banacore, A., Börjesson, P., Bosman, R., Wickstrand, C., Safari, C., … Neutze, R. (2022). Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre. Acta Crystallographica Section D: Structural Biology, 78(6), 698-708. https://doi.org/10.1107/S2059798322004144
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
Cyclic nucleotide-induced helical structure activates a TIR immune effector
Hogrel, G., Guild, A., Graham, S., Rickman, H., Grüschow, S., Bertrand, Q., … White, M. F. (2022). Cyclic nucleotide-induced helical structure activates a TIR immune effector. Nature, 608, 808-812. https://doi.org/10.1038/s41586-022-05070-9
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
Structural basis for receptor selectivity and inverse agonism in S1P<sub>5</sub> receptors
Lyapina, E., Marin, E., Gusach, A., Orekhov, P., Gerasimov, A., Luginina, A., … Cherezov, V. (2022). Structural basis for receptor selectivity and inverse agonism in S1P5 receptors. Nature Communications, 13(1), 4736 (14 pp.). https://doi.org/10.1038/s41467-022-32447-1
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