| Paper | Title | Page |
|---|---|---|
THA01 |
Observations of Fast Structural Changes with an X-ray FEL: Dynamics Studies on Photoactivated Proteins at SACLA | |
|
||
|
X-ray FELs (XFELs) paved the way for exploring ultrafast structural dynamics in a biological macromolecule. Time-resolved protein crystallography with an XFEL now can reach a resolution of the order of femtosecond. One of the most promising techniques for time-resolved measurement is serial femtosecond crystallography (SFX). We have developed an experimental system for time-resolved SFX at SACLA*. This system has been applied for visualizing structural changes in a photoactivated macromolecule such as bacteriorhodopsin (bR)** or photosystem II (PSII)***. In the application to bR, diffraction measurements cover a wide range of timescales from nanoseconds to milliseconds to fully access the structural transitions in the photocycle. The structural data at more than ten time points provided a cascade of structural changes after photoactivation of the retinal chromophore. This 'movie' clearly shows how bR transports protons through a cell membrane against a chemical-potential gradient. This paper gives an overview of the experimental instruments and techniques for studying ultrafast protein dynamics with XFEL, and recent applications at SACLA.
* K. Tono et al., J. Synchrotron Rad. 22, 532 (2015). ** E. Nango et al., Science 354, 1552 (2016). *** M. Suga et al., Nature 543, 131 (2017). |
||
| Export • | reference for this paper using ※ BibTeX, ※ LaTeX, ※ Text/Word, ※ RIS, ※ EndNote (xml) | |