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: | 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 |
Ejemplares similares
-
Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser
por: Wu, Wenting, et al.
Publicado: (2015) -
Possibilities for serial femtosecond crystallography sample delivery at future light sourcesa)
por: Chavas, L. M. G., et al.
Publicado: (2015) -
Room temperature structures beyond 1.5 Å by serial femtosecond crystallography
por: Schmidt, Marius, et al.
Publicado: (2015) -
Improvements in serial femtosecond crystallography of photosystem II by
optimizing crystal uniformity using microseeding procedures
por: Ibrahim, Mohamed, et al.
Publicado: (2015) -
Electronic damage in S atoms in a native protein crystal induced by an
intense X-ray free-electron laser pulse
por: Galli, L., et al.
Publicado: (2015)