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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
Large scale expression and purification of the rat 5-HT<sub>2c</sub> receptor
He, X., Robertson, N., Jazayeri, A., Geroni Gasperina, A., Schertler, G., & Li, X. (2015). Large scale expression and purification of the rat 5-HT2c receptor. Protein Expression and Purification, 106, 1-9. https://doi.org/10.1016/j.pep.2014.10.010
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
Mammalian expression, purification, and crystallization of rhodopsin variants
Mattle, D., Singhal, A., Schmid, G., Dawson, R., & Standfuss, J. (2015). Mammalian expression, purification, and crystallization of rhodopsin variants. In B. Jastrzebska (Ed.), Methods in molecular biology: Vol. 1271. Rhodopsin. Methods and protocols. https://doi.org/10.1007/978-1-4939-2330-4_3
Light-driven Na<sup>+</sup> pumps as next-generation inhibitory optogenetic tools
Nogly, P., & Standfuss, J. (2015). Light-driven Na+ pumps as next-generation inhibitory optogenetic tools. Nature Structural and Molecular Biology, 22(5), 351-353. https://doi.org/10.1038/nsmb.3017
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
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
Viral chemokine mimicry
Standfuss, J. (2015). Viral chemokine mimicry. Science, 347(6226), 1071-1072. https://doi.org/10.1126/science.aaa7998
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
How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation
Abicht, H. K., Schärer, M. A., Quade, N., Ledermann, R., Mohorko, E., Capitani, G., … Glockshuber, R. (2014). How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation. Journal of Biological Chemistry, 289(47), 32431-32444. https://doi.org/10.1074/jbc.M114.607127
Femtosecond X-ray diffraction from two-dimensional protein crystals
Frank, M., Carlson, D. B., Hunter, M. S., Williams, G. J., Messerschmidt, M., Zatsepin, N. A., … Evans, J. E. (2014). Femtosecond X-ray diffraction from two-dimensional protein crystals. IUCrJ, 1, 95-100. https://doi.org/10.1107/S2052252514001444
X-ray structure of the mouse serotonin 5-HT3 receptor
Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M. B., Hovius, R., … Nury, H. (2014). X-ray structure of the mouse serotonin 5-HT3 receptor. Nature, 512(7514), 276-281. https://doi.org/10.1038/nature13552
Crystallization scale preparation of a stable GPCR signaling complex between constitutively active rhodopsin and G-protein
Maeda, S., Sun, D., Singhal, A., Foggetta, M., Schmid, G., Standfuss, J., … Schertler, G. F. X. (2014). Crystallization scale preparation of a stable GPCR signaling complex between constitutively active rhodopsin and G-protein. PLoS One, 9(6), e98714 (11 pp.). https://doi.org/10.1371/journal.pone.0098714
Functional map of arrestin-1 at single amino acid resolution
Ostermaier, M. K., Peterhans, C., Jaussi, R., Deupi, X., & Standfuss, J. (2014). Functional map of arrestin-1 at single amino acid resolution. Proceedings of the National Academy of Sciences of the United States of America PNAS, 111(5), 1825-1830. https://doi.org/10.1073/pnas.1319402111
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
7 Å resolution in protein two-dimensional-crystal X-ray diffraction at Linac Coherent Light Source
Pedrini, B., Tsai, C. J., Capitani, G., Padeste, C., Hunter, M. S., Zatsepin, N. A., … Li, X. D. (2014). 7 Å resolution in protein two-dimensional-crystal X-ray diffraction at Linac Coherent Light Source. Philosophical Transactions of the Royal Society B: Biological Sciences, 369(1647), 20130500 (5 pp.). https://doi.org/10.1098/rstb.2013.0500