scholarly journals Data collection strategies for time-resolved X-ray free-electron laser diffraction, and 2-color methods

2015 ◽  
Vol 2 (4) ◽  
pp. 041714 ◽  
Author(s):  
Chufeng Li ◽  
Kevin Schmidt ◽  
John C. Spence
Keyword(s):  
Data Collection ◽  
Free Electron ◽  
Free Electron Laser ◽  
Laser Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
Collection Strategies

scholarly journals Pump-Probe Time-Resolved Serial Femtosecond Crystallography at SACLA: Current Status and Data Collection Strategies

2019 ◽  
Vol 9 (24) ◽  
pp. 5505 ◽  
Author(s):  
Eriko Nango ◽  
Minoru Kubo ◽  
Kensuke Tono ◽  
So Iwata
Keyword(s):  
Data Collection ◽  
Free Electron ◽  
Free Electron Laser ◽  
Current Status ◽  
Optical Pump ◽  
Time Resolved ◽  
Pump Probe ◽  
X Ray ◽  
Collection Strategies ◽  
Serial Femtosecond Crystallography

Structural information on protein dynamics is a critical factor in fully understanding the protein functions. Pump-probe time-resolved serial femtosecond crystallography (TR-SFX) is a recently established technique for visualizing the structural changes or reactions in proteins that are at work with high spatial and temporal resolution. In the pump-probe method, protein microcrystals are continuously delivered from an injector and exposed to an X-ray free-electron laser (XFEL) pulse after a trigger to initiate a reaction, such as light, chemicals, temperature, and electric field, which affords the structural snapshots of intermediates that occur in the protein. We are in the process of developing the device and techniques for pump-probe TR-SFX while using XFEL produced at SPring-8 Angstrom Compact Free-Electron Laser (SACLA). In this paper, we described our current development details and data collection strategies for the optical pump X-ray probe TR-SFX experiment at SACLA and then reported the techniques of in crystallo TR spectroscopy, which is useful in clarifying the nature of reaction that takes place in crystals in advance.

SAXS Instrumentation

2018 ◽  
Author(s):  
Eaton E. Lattman ◽  
Thomas D. Grant ◽  
Edward H. Snell
Keyword(s):  
Data Collection ◽  
Free Electron ◽  
Free Electron Laser ◽  
Sample Volume ◽  
Time Resolved ◽  
Sample Handling ◽  
X Ray ◽  
Efficient Data ◽  
Laser Sources ◽  
Efficient Data Collection

SAXS instrumentation is available for the laboratory, at the synchrotron, and at X-ray free electron laser sources. This chapter deals with SAXS instrumentation. It covers laboratory systems, synchrotron beamlines and newer sources. Multiple synchrotron facilities have SAXS beamlines and the ability to perform SAXS studies on free electron laser sources is growing. Sample handling has adopted automation and in some cases microfluidics to reduce sample volume requirements. Sensitive detectors efficient data collection software and rapid analysis allow real time decisions to be made during data collection. Specialized apparatus enables time resolved studies. Each component is described.

Time-Resolved Serial Femtosecond Crystallography at the European X-ray Free Electron Laser

2019 ◽  
Author(s):  
Marius Schmidt ◽  
Suraj Pandey ◽  
Adrian Mancuso ◽  
Richard Bean
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Crystallographic Data ◽  
Time Resolved ◽  
X Ray ◽  
Serial Femtosecond Crystallography

Abstract This protocol introduces step by step into the collection of time resolved crystallographic data and their analysis at the European Free Electron Laser.

scholarly journals Two mirror X-ray pulse split and delay instrument for femtosecond time resolved investigations at the LCLS free electron laser facility

2016 ◽  
Vol 24 (11) ◽  
pp. 11768 ◽  
Author(s):  
Nora Berrah ◽  
Li Fang ◽  
Brendan F Murphy ◽  
Edwin Kukk ◽  
Timur Y. Osipov ◽  
...  
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Time Resolved ◽  
X Ray ◽  
Laser Facility

scholarly journals Direct autocorrelation of soft-x-ray free-electron-laser pulses by time-resolved two-photon double ionization of He

2009 ◽  
Vol 80 (2) ◽  
Author(s):  
R. Mitzner ◽  
A. A. Sorokin ◽  
B. Siemer ◽  
S. Roling ◽  
M. Rutkowski ◽  
...  
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Laser Pulses ◽  
Double Ionization ◽  
Time Resolved ◽  
X Ray ◽  
Two Photon

scholarly journals Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laser

2015 ◽  
Vol 71 (7) ◽  
pp. 856-860 ◽  
Author(s):  
Wenting Wu ◽  
Przemyslaw Nogly ◽  
Jan Rheinberger ◽  
Leonhard M. Kick ◽  
Cornelius Gati ◽  
...  
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Second Harmonic ◽  
Night Vision ◽  
Salt Crystallization ◽  
Time Resolved ◽  
Batch Crystallization ◽  
X Ray ◽  
Vapour Diffusion ◽  
Serial Crystallography

Rhodopsin is a membrane protein from the G protein-coupled receptor family. Together with its ligand retinal, it forms the visual pigment responsible for night vision. In order to perform ultrafast dynamics studies, a time-resolved serial femtosecond crystallography method is required owing to the nonreversible activation of rhodopsin. In such an approach, microcrystals in suspension are delivered into the X-ray pulses of an X-ray free-electron laser (XFEL) after a precise photoactivation delay. Here, a millilitre batch production of high-density microcrystals was developed by four methodical conversion steps starting from known vapour-diffusion crystallization protocols: (i) screening the low-salt crystallization conditions preferred for serial crystallography by vapour diffusion, (ii) optimization of batch crystallization, (iii) testing the crystal size and quality using second-harmonic generation (SHG) imaging and X-ray powder diffraction and (iv) production of millilitres of rhodopsin crystal suspension in batches for serial crystallography tests; these crystals diffracted at an XFEL at the Linac Coherent Light Source using a liquid-jet setup.

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