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Keywords = TR-SFX

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13 pages, 3379 KiB  
Article
Linear and Non-Linear Population Retrieval with Femtosecond Optical Pumping of Molecular Crystals for the Generalised Uniaxial and Biaxial Systems
by Christopher D. M. Hutchison, Alisia Fadini and Jasper J. van Thor
Appl. Sci. 2022, 12(9), 4309; https://doi.org/10.3390/app12094309 - 24 Apr 2022
Cited by 1 | Viewed by 3023
Abstract
Femtosecond optical measurements of photoexcitable molecular crystals carry ultrafast dynamics information with structural sensitivity. The creation and detection of transient dynamics depend on the optical parameters, as well as the explicit molecular structure, crystal symmetry, crystal orientation, polarisation of the photoexciting beam, and [...] Read more.
Femtosecond optical measurements of photoexcitable molecular crystals carry ultrafast dynamics information with structural sensitivity. The creation and detection of transient dynamics depend on the optical parameters, as well as the explicit molecular structure, crystal symmetry, crystal orientation, polarisation of the photoexciting beam, and interaction geometry. In order to retrieve the linear and non-linear population transfer in photoexcited crystals, excitation theory is combined here with the calculation of birefringence decomposition and is shown for both the generalised uniaxial and biaxial systems. A computational tool was constructed based on this treatment to allow modelling of electric field decomposition, dipole projections, and non-linear excitation population levels. This is available open source and with a GUI for ease of use. Such work has applications in two areas of ultrafast science: multidimensional optical crystallography and femtosecond time-resolved X-ray crystallography. Full article
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12 pages, 931 KiB  
Perspective
Potential of Time-Resolved Serial Femtosecond Crystallography Using High Repetition Rate XFEL Sources
by Raphaël de Wijn, Diogo V. M. Melo, Faisal H. M. Koua and Adrian P. Mancuso
Appl. Sci. 2022, 12(5), 2551; https://doi.org/10.3390/app12052551 - 28 Feb 2022
Cited by 16 | Viewed by 3974
Abstract
This perspective review describes emerging techniques and future opportunities for time-resolved serial femtosecond crystallography (TR-SFX) experiments using high repetition rate XFEL sources. High repetition rate sources are becoming more available with the European XFEL in operation and the recently upgraded LCLS-II will be [...] Read more.
This perspective review describes emerging techniques and future opportunities for time-resolved serial femtosecond crystallography (TR-SFX) experiments using high repetition rate XFEL sources. High repetition rate sources are becoming more available with the European XFEL in operation and the recently upgraded LCLS-II will be available in the near future. One efficient use of these facilities for TR-SFX relies on pump–probe experiments using a laser to trigger a reaction of light-responsive proteins or mix-and-inject experiments for light-unresponsive proteins. With the view to widen the application of TR-SFX, the promising field of photocaged compounds is under development, which allows the very fast laser triggering of reactions that is no longer limited to naturally light-responsive samples. In addition to reaction triggering, a key concern when performing an SFX experiment is efficient sample usage, which is a main focus of new high repetition rate-compatible sample delivery methods. Full article
(This article belongs to the Special Issue Latest Trends in Free Electron Lasers)
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22 pages, 3619 KiB  
Review
Protein Dynamics and Time Resolved Protein Crystallography at Synchrotron Radiation Sources: Past, Present and Future
by Jose M. Martin-Garcia
Crystals 2021, 11(5), 521; https://doi.org/10.3390/cryst11050521 - 8 May 2021
Cited by 28 | Viewed by 5960
Abstract
The ultrabright and ultrashort pulses produced at X-ray free electron lasers (XFELs) has enabled studies of crystallized molecular machines at work under ‘native’ conditions at room temperature by the so-called time-resolved serial femtosecond crystallography (TR-SFX) technique. Since early TR-SFX experiments were conducted at [...] Read more.
The ultrabright and ultrashort pulses produced at X-ray free electron lasers (XFELs) has enabled studies of crystallized molecular machines at work under ‘native’ conditions at room temperature by the so-called time-resolved serial femtosecond crystallography (TR-SFX) technique. Since early TR-SFX experiments were conducted at XFELs, it has been largely reported in the literature that time-resolved X-ray experiments at synchrotrons are no longer feasible or are impractical due to the severe technical limitations of these radiation sources. The transfer of the serial crystallography approach to newest synchrotrons upgraded for higher flux density and with beamlines using sophisticated focusing optics, submicron beam diameters and fast low-noise photon-counting detectors offers a way to overcome these difficulties opening new and exciting possibilities. In fact, there is an increasing amount of publications reporting new findings in structural dynamics of protein macromolecules by using time resolved crystallography from microcrystals at synchrotron sources. This review gathers information to provide an overview of the recent work and the advances made in this filed in the past years, as well as outlines future perspectives at the next generation of synchrotron sources and the upcoming compact pulsed X-ray sources. Full article
(This article belongs to the Special Issue Approach of Serial Crystallography)
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11 pages, 1702 KiB  
Review
Pump-Probe Time-Resolved Serial Femtosecond Crystallography at SACLA: Current Status and Data Collection Strategies
by Eriko Nango, Minoru Kubo, Kensuke Tono and So Iwata
Appl. Sci. 2019, 9(24), 5505; https://doi.org/10.3390/app9245505 - 14 Dec 2019
Cited by 10 | Viewed by 5075
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Science at X-ray Free Electron Lasers)
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