scholarly journals Self-synchronized and cost-effective time-resolved measurements at x-ray free-electron lasers with femtosecond resolution

2022 ◽  
Vol 4 (1) ◽  
Author(s):  
Philipp Dijkstal ◽  
Alexander Malyzhenkov ◽  
Paolo Craievich ◽  
Eugenio Ferrari ◽  
Romain Ganter ◽  
...  
2014 ◽  
Vol 5 (1) ◽  
Author(s):  
C. Behrens ◽  
F.-J. Decker ◽  
Y. Ding ◽  
V. A. Dolgashev ◽  
J. Frisch ◽  
...  

2019 ◽  
Vol 20 (6) ◽  
pp. 1401 ◽  
Author(s):  
Marius Schmidt

The focus of structural biology is shifting from the determination of static structures to the investigation of dynamical aspects of macromolecular function. With time-resolved macromolecular crystallography (TRX), intermediates that form and decay during the macromolecular reaction can be investigated, as well as their reaction dynamics. Time-resolved crystallographic methods were initially developed at synchrotrons. However, about a decade ago, extremely brilliant, femtosecond-pulsed X-ray sources, the free electron lasers for hard X-rays, became available to a wider community. TRX is now possible with femtosecond temporal resolution. This review provides an overview of methodological aspects of TRX, and at the same time, aims to outline the frontiers of this method at modern pulsed X-ray sources.


2011 ◽  
Vol 98 (18) ◽  
pp. 182504 ◽  
Author(s):  
N. Pontius ◽  
T. Kachel ◽  
C. Schüßler-Langeheine ◽  
W. F. Schlotter ◽  
M. Beye ◽  
...  

2016 ◽  
Vol 3 (5) ◽  
pp. 054301 ◽  
Author(s):  
George D. Calvey ◽  
Andrea M. Katz ◽  
Chris B. Schaffer ◽  
Lois Pollack

2020 ◽  
Vol 10 (10) ◽  
pp. 3642 ◽  
Author(s):  
Grant Mills ◽  
Richard Bean ◽  
Adrian P. Mancuso

Ultrabright pulses produced in X-ray free-electron lasers (XFELs) offer new possibilities for industry and research, particularly for biochemistry and pharmaceuticals. The unprecedented brilliance of these next-generation sources enables structure determination from sub-micron crystals as well as radiation-sensitive proteins. The European X-Ray Free-Electron Laser (EuXFEL), with its first light in 2017, ushered in a new era for ultrabright X-ray sources by providing an unparalleled megahertz-pulse repetition rate, with orders of magnitude more pulses per second than previous XFEL sources. This rapid pulse frequency has significant implications for structure determination; not only will data collection be faster (resulting in more structures per unit time), but experiments requiring large quantities of data, such as time-resolved structures, become feasible in a reasonable amount of experimental time. Early experiments at the SPB/SFX instrument of the EuXFEL demonstrate how such closely-spaced pulses can be successfully implemented in otherwise challenging experiments, such as time-resolved studies.


Crystals ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 628
Author(s):  
Suraj Pandey ◽  
Ishwor Poudyal ◽  
Tek Narsingh Malla

With time-resolved crystallography (TRX), it is possible to follow the reaction dynamics in biological macromolecules by investigating the structure of transient states along the reaction coordinate. X-ray free electron lasers (XFELs) have enabled TRX experiments on previously uncharted femtosecond timescales. Here, we review the recent developments, opportunities, and challenges of pump-probe TRX at XFELs.


2017 ◽  
Vol 50 (3) ◽  
pp. 909-918 ◽  
Author(s):  
Nadia Opara ◽  
Isabelle Martiel ◽  
Stefan A. Arnold ◽  
Thomas Braun ◽  
Henning Stahlberg ◽  
...  

A new era of protein crystallography started when X-ray free-electron lasers (XFELs) came into operation, as these provide an intense source of X-rays that facilitates data collection in the `diffract-before-destroy' regime. In typical experiments, crystals sequentially delivered to the beam are exposed to X-rays and destroyed. Therefore, the novel approach of serial crystallography requires thousands of nearly identical samples. Currently applied sample-delivery methods, in particular liquid jets or drop-on-demand systems, suffer from significant sample consumption of the precious crystalline material. Direct protein microcrystal growth by the vapour diffusion technique inside arrays of nanolitre-sized wells is a method specifically tailored to crystallography at XFELs. The wells, with X-ray transparent Si3N4windows as bottoms, are fabricated in silicon chips. Their reduced dimensions can significantly decrease protein specimen consumption. Arrays provide crystalline samples positioned in an ordered way without the need to handle fragile crystals. The nucleation process inside these microfabricated cavities was optimized to provide high membrane coverage and a quasi-random crystal distribution. Tight sealing of the chips and protection of the crystals from dehydration were achieved, as confirmed by diffraction experiments at a protein crystallography beamline. Finally, the test samples were shown to be suitable for time-resolved measurements at an XFEL at femtosecond resolution.


2005 ◽  
Vol 12 (6) ◽  
pp. 812-819 ◽  
Author(s):  
C. Blome ◽  
Th. Tschentscher ◽  
J. Davaasambuu ◽  
P. Durand ◽  
S. Techert

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