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Time-resolved structural studies with serial crystallography: A new light on retinal proteins

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 de...

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Autores principales: Panneels, Valérie, Wu, Wenting, Tsai, Ching-Ju, Nogly, Przemek, Rheinberger, Jan, Jaeger, Kathrin, Cicchetti, Gregor, Gati, Cornelius, Kick, Leonhard M., Sala, Leonardo, Capitani, Guido, Milne, Chris, Padeste, Celestino, Pedrini, Bill, Li, Xiao-Dan, Standfuss, Jörg, Abela, Rafael, Schertler, Gebhard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Crystallographic Association 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711639/
https://www.ncbi.nlm.nih.gov/pubmed/26798817
http://dx.doi.org/10.1063/1.4922774
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author Panneels, Valérie
Wu, Wenting
Tsai, Ching-Ju
Nogly, Przemek
Rheinberger, Jan
Jaeger, Kathrin
Cicchetti, Gregor
Gati, Cornelius
Kick, Leonhard M.
Sala, Leonardo
Capitani, Guido
Milne, Chris
Padeste, Celestino
Pedrini, Bill
Li, Xiao-Dan
Standfuss, Jörg
Abela, Rafael
Schertler, Gebhard
author_facet Panneels, Valérie
Wu, Wenting
Tsai, Ching-Ju
Nogly, Przemek
Rheinberger, Jan
Jaeger, Kathrin
Cicchetti, Gregor
Gati, Cornelius
Kick, Leonhard M.
Sala, Leonardo
Capitani, Guido
Milne, Chris
Padeste, Celestino
Pedrini, Bill
Li, Xiao-Dan
Standfuss, Jörg
Abela, Rafael
Schertler, Gebhard
author_sort Panneels, Valérie
collection PubMed
description 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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spelling pubmed-47116392016-01-21 Time-resolved structural studies with serial crystallography: A new light on retinal proteins Panneels, Valérie Wu, Wenting Tsai, Ching-Ju Nogly, Przemek Rheinberger, Jan Jaeger, Kathrin Cicchetti, Gregor Gati, Cornelius Kick, Leonhard M. Sala, Leonardo Capitani, Guido Milne, Chris Padeste, Celestino Pedrini, Bill Li, Xiao-Dan Standfuss, Jörg Abela, Rafael Schertler, Gebhard Struct Dyn SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2 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. American Crystallographic Association 2015-06-29 /pmc/articles/PMC4711639/ /pubmed/26798817 http://dx.doi.org/10.1063/1.4922774 Text en © 2015 Author(s). 2329-7778/2015/2(4)/041718/8 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License.
spellingShingle SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2
Panneels, Valérie
Wu, Wenting
Tsai, Ching-Ju
Nogly, Przemek
Rheinberger, Jan
Jaeger, Kathrin
Cicchetti, Gregor
Gati, Cornelius
Kick, Leonhard M.
Sala, Leonardo
Capitani, Guido
Milne, Chris
Padeste, Celestino
Pedrini, Bill
Li, Xiao-Dan
Standfuss, Jörg
Abela, Rafael
Schertler, Gebhard
Time-resolved structural studies with serial crystallography: A new light on retinal proteins
title Time-resolved structural studies with serial crystallography: A new light on retinal proteins
title_full Time-resolved structural studies with serial crystallography: A new light on retinal proteins
title_fullStr Time-resolved structural studies with serial crystallography: A new light on retinal proteins
title_full_unstemmed Time-resolved structural studies with serial crystallography: A new light on retinal proteins
title_short Time-resolved structural studies with serial crystallography: A new light on retinal proteins
title_sort time-resolved structural studies with serial crystallography: a new light on retinal proteins
topic SPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4711639/
https://www.ncbi.nlm.nih.gov/pubmed/26798817
http://dx.doi.org/10.1063/1.4922774
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