X-ray Free Electron Lasers Motivate Bioanalytical Characterization of Protein Nanocrystals: Serial Femtosecond Crystallography

2013 ◽  
Vol 85 (7) ◽  
pp. 3464-3471 ◽  
Author(s):  
Michael J. Bogan
2014 ◽  
Vol 369 (1647) ◽  
pp. 20130337 ◽  
Author(s):  
Uwe Weierstall

X-ray free-electron lasers overcome the problem of radiation damage in protein crystallography and allow structure determination from micro- and nanocrystals at room temperature. To ensure that consecutive X-ray pulses do not probe previously exposed crystals, the sample needs to be replaced with the X-ray repetition rate, which ranges from 120 Hz at warm linac-based free-electron lasers to 1 MHz at superconducting linacs. Liquid injectors are therefore an essential part of a serial femtosecond crystallography experiment at an X-ray free-electron laser. Here, we compare different techniques of injecting microcrystals in solution into the pulsed X-ray beam in vacuum. Sample waste due to mismatch of the liquid flow rate to the X-ray repetition rate can be addressed through various techniques.


Author(s):  
Takashi Tanaka ◽  
Shunji Goto ◽  
Toru Hara ◽  
Takaki Hatsui ◽  
Haruhiko Ohashi ◽  
...  

2019 ◽  
Vol 123 (23) ◽  
Author(s):  
E. Prat ◽  
P. Dijkstal ◽  
M. Aiba ◽  
S. Bettoni ◽  
P. Craievich ◽  
...  

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.


RSC Advances ◽  
2020 ◽  
Vol 10 (27) ◽  
pp. 15694-15701
Author(s):  
Majid Hejazian ◽  
Connie Darmanin ◽  
Eugeniu Balaur ◽  
Brian Abbey

Design schematics of microfluidic mix- and-jet devices for serial femtosecond crystallography (SFX) at X-ray free electron lasers (XFELs).


2014 ◽  
Vol 369 (1647) ◽  
pp. 20130318 ◽  
Author(s):  
Richard Neutze

X-ray free-electron lasers (XFELs) are revolutionary X-ray sources. Their time structure, providing X-ray pulses of a few tens of femtoseconds in duration; and their extreme peak brilliance, delivering approximately 10 12 X-ray photons per pulse and facilitating sub-micrometre focusing, distinguish XFEL sources from synchrotron radiation. In this opinion piece, I argue that these properties of XFEL radiation will facilitate new discoveries in life science. I reason that time-resolved serial femtosecond crystallography and time-resolved wide angle X-ray scattering are promising areas of scientific investigation that will be advanced by XFEL capabilities, allowing new scientific questions to be addressed that are not accessible using established methods at storage ring facilities. These questions include visualizing ultrafast protein structural dynamics on the femtosecond to picosecond time-scale, as well as time-resolved diffraction studies of non-cyclic reactions. I argue that these emerging opportunities will stimulate a renaissance of interest in time-resolved structural biochemistry.


2016 ◽  
Vol 3 (3) ◽  
pp. 034301 ◽  
Author(s):  
Tetsuo Katayama ◽  
Shigeki Owada ◽  
Tadashi Togashi ◽  
Kanade Ogawa ◽  
Petri Karvinen ◽  
...  

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