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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
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, (144), e59087. 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
Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography
Weinert, T., Skopintsev, P., James, D., Dworkowski, F., Panepucci, E., Kekilli, D., … Standfuss, J. (2019). Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science, 365(6448), 61-65. https://doi.org/10.1126/science.aaw8634
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
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
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
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
Serial millisecond crystallography of membrane proteins
Jaeger, K., Dworkowski, F., Nogly, P., Milne, C., Wang, M., & Standfuss, J. (2016). Serial millisecond crystallography of membrane proteins. In I. Moraes (Ed.), Advances in experimental medicine and biology: Vol. 922. The next generation in membrane protein structure determination. https://doi.org/10.1007/978-3-319-35072-1_10
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
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
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Kang, Y., Zhou, X. E., Gao, X., He, Y., Liu, W., Ishchenko, A., … Xu, H. E. (2015). Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature, 523, 561-567. https://doi.org/10.1038/nature14656