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	Strategic screening and characterization of the visual GPCR-mini-G protein signaling complex for successful crystallization Pamula, F., Mühle, J., Blanc, A., Nehmé, R., Edwards, P. C., Tate, C. G., & Tsai, C. J. (2020). Strategic screening and characterization of the visual GPCR-mini-G protein signaling complex for successful crystallization. Journal of Visualized Experiments, 2020(157), e60747 (10 pp.). https://doi.org/10.3791/60747 Detailed Record Published Version
	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 Detailed Record Published Version
	Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit Tsai, C. J., Marino, J., Adaixo, R., Pamula, F., Muehle, J., Maeda, S., … Schertler, G. (2019). Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. eLife, 8, e46041 (19 pp.). https://doi.org/10.7554/eLife.46041 Detailed Record Published Version Accepted Version
	Structure of the μ–opioid receptor–G<sub>i</sub> protein complex Koehl, A., Hu, H., Maeda, S., Zhang, Y., Qu, Q., Paggi, J. M., … Kobilka, B. K. (2018). Structure of the μ–opioid receptor–G_i protein complex. Nature, 558(7711), 547-552. https://doi.org/10.1038/s41586-018-0219-7 Detailed Record Published Version
	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 Detailed Record Published Version
	Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser Nogly, P., Weinert, T., James, D., Carbajo, S., Ozerov, D., Furrer, A., … Standfuss, J. (2018). Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science, 361(6398), eaat0094 (7 pp.). https://doi.org/10.1126/science.aat0094 Detailed Record Published Version Accepted Version
	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-G_o sheds light on the principles of G protein selectivity. Science Advances, 4(9), aat7052 (9 pp.). https://doi.org/10.1126/sciadv.aat7052 Detailed Record Published Version
	Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons Weinert, T., Olieric, N., Cheng, R., Brünle, S., James, D., Ozerov, D., … Standfuss, J. (2017). Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nature Communications, 8(1), 542 (11 pp.). https://doi.org/10.1038/s41467-017-00630-4 Detailed Record Published Version
	Backbone NMR reveals allosteric signal transduction networks in the β<sub>1</sub>-adrenergic receptor Isogai, S., Deupi, X., Opitz, C., Heydenreich, F. M., Tsai, C. J., Brueckner, F., … Grzesiek, S. (2016). Backbone NMR reveals allosteric signal transduction networks in the β₁-adrenergic receptor. Nature, 530(7589), 237-241. https://doi.org/10.1038/nature16577 Detailed Record Published Version
	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 Detailed Record Published Version Accepted Version Supplemental Material
	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 Detailed Record Published Version
	Structural role of the T94I rhodopsin mutation in congenital stationary night blindness Singhal, A., Guo, Y., Matkovic, M., Schertler, G., Deupi, X., Yan, E. C. Y., & Standfuss, J. (2016). Structural role of the T94I rhodopsin mutation in congenital stationary night blindness. EMBO Reports, 17(10), 1431-1440. https://doi.org/10.15252/embr.201642671 Detailed Record Published Version
	Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region Venkatakrishnan, A. J., Deupi, X., Lebon, G., Heydenreich, F. M., Flock, T., Miljus, T., … Babu, M. M. (2016). Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region. Nature, 536(7617), 484-487. https://doi.org/10.1038/nature19107 Detailed Record Published Version
	Membrane protein structural biology using X-ray free electron lasers Neutze, R., Brändén, G., & Schertler, G. F. X. (2015). Membrane protein structural biology using X-ray free electron lasers. Current Opinion in Structural Biology, 33, 115-125. https://doi.org/10.1016/j.sbi.2015.08.006 Detailed Record Published Version
	Lipidic cubic phase serial millisecond crystallography using synchrotron radiation Nogly, P., James, D., Wang, D., White, T. A., Zatsepin, N., Shilova, A., … Weierstall, U. (2015). Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. IUCrJ, 2, 168-176. https://doi.org/10.1107/S2052252514026487 Detailed Record Published Version
	Time-resolved structural studies with serial crystallography: a new light on retinal proteins Panneels, V., Wu, W., Tsai, C. J., Nogly, P., Rheinberger, J., Jaeger, K., … Schertler, G. (2015). Time-resolved structural studies with serial crystallography: a new light on retinal proteins. Structural Dynamics, 2(4), 041718 (8 pp.). https://doi.org/10.1063/1.4922774 Detailed Record Published Version
	Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser Wu, W., Nogly, P., Rheinberger, J., Kick, L. M., Gati, C., Nelson, G., … Panneels, V. (2015). Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 71, 856-860. https://doi.org/10.1107/S2053230X15009966 Detailed Record Published Version
	Molecular mechanism of phosphorylation-dependent arrestin activation Ostermaier, M. K., Schertler, G. F. X., & Standfuss, J. (2014). Molecular mechanism of phosphorylation-dependent arrestin activation. Current Opinion in Structural Biology, 29, 143-151. https://doi.org/10.1016/j.sbi.2014.07.006 Detailed Record Published Version