Cargando…
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...
Autores principales: | , , , , , , , , , , , , , , , , , |
---|---|
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 |
_version_ | 1782409964556386304 |
---|---|
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. |
format | Online Article Text |
id | pubmed-4711639 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American Crystallographic Association |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT panneelsvalerie timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT wuwenting timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT tsaichingju timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT noglyprzemek timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT rheinbergerjan timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT jaegerkathrin timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT cicchettigregor timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT gaticornelius timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT kickleonhardm timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT salaleonardo timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT capitaniguido timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT milnechris timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT padestecelestino timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT pedrinibill timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT lixiaodan timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT standfussjorg timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT abelarafael timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins AT schertlergebhard timeresolvedstructuralstudieswithserialcrystallographyanewlightonretinalproteins |