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000275873 041__ $$aEnglish
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000275873 1001_ $$0P:(DE-HGF)0$$aPanneels, Valérie$$b0
000275873 245__ $$aTime-resolved structural studies with serial crystallography: A new light on retinal proteins
000275873 260__ $$aMelville, NY$$bAIP Publishing LLC$$c2015
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000275873 520__ $$aStructural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, these methods do not allow for the structure determination of most intermediate conformations. Recently, the potential of X-Ray Free Electron Lasers (X-FELs) for tracking the dynamics of light-triggered processes by pump-probe serial femtosecond crystallography has been demonstrated using 3D-micron-sized crystals. In addition, X-FELs provide new opportunities for protein 2D-crystal diffraction, which would allow to observe the course of conformational changes of membrane proteins in a close-to-physiological lipid bilayer environment. Here, we describe the strategies towards structural dynamic studies of retinal proteins at room temperature, using injector or fixed-target based serial femtosecond crystallography at X-FELs. Thanks to recent progress especially in sample delivery methods, serial crystallography is now also feasible at synchrotron X-ray sources, thus expanding the possibilities for time-resolved structure determination.
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000275873 536__ $$0G:(EU-Grant)317079$$aNANOMEM - Membrane Protein Nanocrystallography (317079)$$c317079$$fFP7-PEOPLE-2012-ITN$$x1
000275873 536__ $$0G:(EU-Grant)637295$$aX-probe - Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics (637295)$$c637295$$fH2020-MSCA-ITN-2014$$x2
000275873 536__ $$0G:(DE-HGF)2015_IFV-VH-GS-500$$aVH-GS-500 - PIER Helmholtz Graduate School (2015_IFV-VH-GS-500)$$c2015_IFV-VH-GS-500$$x3
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000275873 7001_ $$0P:(DE-HGF)0$$aWu, Wenting$$b1
000275873 7001_ $$0P:(DE-HGF)0$$aTsai, Ching-Ju$$b2
000275873 7001_ $$0P:(DE-HGF)0$$aNogly, Przemek$$b3
000275873 7001_ $$0P:(DE-HGF)0$$aRheinberger, Jan$$b4
000275873 7001_ $$0P:(DE-HGF)0$$aJaeger, Kathrin$$b5
000275873 7001_ $$0P:(DE-HGF)0$$aCicchetti, Gregor$$b6
000275873 7001_ $$0P:(DE-H253)PIP1017962$$aGati, Cornelius$$b7
000275873 7001_ $$0P:(DE-HGF)0$$aKick, Leonhard M.$$b8
000275873 7001_ $$0P:(DE-HGF)0$$aSala, Leonardo$$b9
000275873 7001_ $$0P:(DE-HGF)0$$aCapitani, Guido$$b10
000275873 7001_ $$0P:(DE-HGF)0$$aMilne, Chris$$b11
000275873 7001_ $$0P:(DE-HGF)0$$aPadeste, Celestino$$b12
000275873 7001_ $$0P:(DE-HGF)0$$aPedrini, Bill$$b13
000275873 7001_ $$0P:(DE-HGF)0$$aLi, Xiao-Dan$$b14
000275873 7001_ $$0P:(DE-HGF)0$$aStandfuss, Jörg$$b15
000275873 7001_ $$0P:(DE-HGF)0$$aAbela, Rafael$$b16
000275873 7001_ $$0P:(DE-HGF)0$$aSchertler, Gebhard$$b17$$eCorresponding author
000275873 773__ $$0PERI:(DE-600)2758684-4$$a10.1063/1.4922774$$gVol. 2, no. 4, p. 041718 -$$n4$$p041718$$tStructural dynamics$$v2$$x2329-7778$$y2015
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000275873 9141_ $$y2015
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