| Activating an invertebrate bistable opsin with the all-trans 6.11 retinal analog
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| Continuous population-level monitoring of SARS-CoV-2 seroprevalence in a large European metropolitan region
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| Ultrafast structural changes direct the first molecular events of vision
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| Preparation of a stable CCL5·CCR5·G<sub>i</sub> signaling complex for cryo-EM analysis
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| Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist
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| Versatile microporous polymer-based supports for serial macromolecular crystallography
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| Biochemical characterization of GPCR-G protein complex formation
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| High-mass MALDI-MS unravels ligand-mediated G protein-coupling selectivity to GPCRs
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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 |
| GPCR activation states induced by nanobodies and mini-G proteins compared by NMR spectroscopy
Rößler, P., Mayer, D., Tsai, C. J., Veprintsev, D. B., Schertler, G. F. X., & Gossert, A. D. (2020). GPCR activation states induced by nanobodies and mini-G proteins compared by NMR spectroscopy. Molecules, 25(24), 5984 (17 pp.). https://doi.org/10.3390/molecules25245984 |
| Membrane protein crystallization
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| Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals
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| Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit
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| Emerging two-dimensional crystallization of cucurbit[8]uril complexes: from supramolecular polymers to nanofibers
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| Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals
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| 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 |
| Structural biology: signalling under the microscope
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| Backbone NMR reveals allosteric signal transduction networks in the β<sub>1</sub>-adrenergic receptor
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| Low-<em>Z</em> polymer sample supports for fixed-target serial femtosecond X-ray crystallography
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| Time-resolved structural studies with serial crystallography: a new light on retinal proteins
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