| Home > Publications database > Time-resolved structural studies with serial crystallography: A new light on retinal proteins > print |
| 001 | 275873 | ||
| 005 | 20250730113436.0 | ||
| 024 | 7 | _ | |a 10.1063/1.4922774 |2 doi |
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| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 530 |
| 100 | 1 | _ | |a Panneels, Valérie |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Time-resolved structural studies with serial crystallography: A new light on retinal proteins |
| 260 | _ | _ | |a Melville, NY |c 2015 |b AIP Publishing LLC |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, these methods do not allow for the structure determination of most intermediate conformations. Recently, the potential of X-Ray Free Electron Lasers (X-FELs) for tracking the dynamics of light-triggered processes by pump-probe serial femtosecond crystallography has been demonstrated using 3D-micron-sized crystals. In addition, X-FELs provide new opportunities for protein 2D-crystal diffraction, which would allow to observe the course of conformational changes of membrane proteins in a close-to-physiological lipid bilayer environment. Here, we describe the strategies towards structural dynamic studies of retinal proteins at room temperature, using injector or fixed-target based serial femtosecond crystallography at X-FELs. Thanks to recent progress especially in sample delivery methods, serial crystallography is now also feasible at synchrotron X-ray sources, thus expanding the possibilities for time-resolved structure determination. |
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| 536 | _ | _ | |a NANOMEM - Membrane Protein Nanocrystallography (317079) |0 G:(EU-Grant)317079 |c 317079 |f FP7-PEOPLE-2012-ITN |x 1 |
| 536 | _ | _ | |a X-probe - Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics (637295) |0 G:(EU-Grant)637295 |c 637295 |f H2020-MSCA-ITN-2014 |x 2 |
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| 700 | 1 | _ | |a Wu, Wenting |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Tsai, Ching-Ju |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Nogly, Przemek |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Rheinberger, Jan |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Jaeger, Kathrin |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Cicchetti, Gregor |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Gati, Cornelius |0 P:(DE-H253)PIP1017962 |b 7 |
| 700 | 1 | _ | |a Kick, Leonhard M. |0 P:(DE-HGF)0 |b 8 |
| 700 | 1 | _ | |a Sala, Leonardo |0 P:(DE-HGF)0 |b 9 |
| 700 | 1 | _ | |a Capitani, Guido |0 P:(DE-HGF)0 |b 10 |
| 700 | 1 | _ | |a Milne, Chris |0 P:(DE-HGF)0 |b 11 |
| 700 | 1 | _ | |a Padeste, Celestino |0 P:(DE-HGF)0 |b 12 |
| 700 | 1 | _ | |a Pedrini, Bill |0 P:(DE-HGF)0 |b 13 |
| 700 | 1 | _ | |a Li, Xiao-Dan |0 P:(DE-HGF)0 |b 14 |
| 700 | 1 | _ | |a Standfuss, Jörg |0 P:(DE-HGF)0 |b 15 |
| 700 | 1 | _ | |a Abela, Rafael |0 P:(DE-HGF)0 |b 16 |
| 700 | 1 | _ | |a Schertler, Gebhard |0 P:(DE-HGF)0 |b 17 |e Corresponding author |
| 773 | _ | _ | |a 10.1063/1.4922774 |g Vol. 2, no. 4, p. 041718 - |0 PERI:(DE-600)2758684-4 |n 4 |p 041718 |t Structural dynamics |v 2 |y 2015 |x 2329-7778 |
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