scholarly journals X-ray diffraction in temporally and spatially resolved biomolecular science

2015 ◽  
Vol 177 ◽  
pp. 429-441 ◽  
Author(s):  
John R. Helliwell ◽  
Alice Brink ◽  
Surasak Kaenket ◽  
Victoria Laurina Starkey ◽  
Simon W. M. Tanley
Keyword(s):  
Single Molecule ◽  
Structural Changes ◽  
Protein Crystallography ◽  
European Synchrotron Radiation Facility ◽  
Protein Crystal ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Microscopy Imaging ◽  
Time Resolved ◽  
X Ray

Time-resolved Laue protein crystallography at the European Synchrotron Radiation Facility (ESRF) opened up the field of sub-nanosecond protein crystal structure analyses. There are a limited number of such time-resolved studies in the literature. Why is this? The X-ray laser now gives us femtosecond (fs) duration pulses, typically 10 fs up to ∼50 fs. Their use is attractive for the fastest time-resolved protein crystallography studies. It has been proposed that single molecules could even be studied with the advantage of being able to measure X-ray diffraction from a ‘crystal lattice free’ single molecule, with or without temporal resolved structural changes. This is altogether very challenging R&D. So as to assist this effort we have undertaken studies of metal clusters that bind to proteins, both ‘fresh’ and after repeated X-ray irradiation to assess their X-ray-photo-dynamics, namely Ta6Br12, K2PtI6 and K2PtBr6 bound to a test protein, hen egg white lysozyme. These metal complexes have the major advantage of being very recognisable shapes (pseudo spherical or octahedral) and thereby offer a start to (probably very difficult) single molecule electron density map interpretations, both static and dynamic. A further approach is to investigate the X-ray laser beam diffraction strength of a well scattering nano-cluster; an example from nature being the iron containing ferritin. Electron crystallography and single particle electron microscopy imaging offers alternatives to X-ray structural studies; our structural studies of crustacyanin, a 320 kDa protein carotenoid complex, can be extended either by electron based techniques or with the X-ray laser representing a fascinating range of options. General outlook remarks concerning X-ray, electron and neutron macromolecular crystallography as well as ‘NMR crystallography’ conclude the article.

scholarly journals On the possibility of the Observation of Intramolecular Reaction Dynamics in Liquids by Time-resolved X-ray Scattering

2002 ◽  
Vol 216 (5) ◽  
Author(s):  
S. Techert ◽  
S. Schmatz
Keyword(s):  
Gas Phase ◽  
Free Electron Laser ◽  
Structural Changes ◽  
Reaction Dynamics ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Trans Stilbene

The feasibility of time-resolved structural studies using pulsed X-ray radiation from a 3rd generation synchrotron is discussed and compared with scattering experiments which might be possible with a future free electron laser (X-FEL). As an example, it is shown that the structural changes during the isomerisation process of trans-stilbene into cis-stilbene can be observed using time-resolved X-ray diffraction in the gas-phase as well as in solution.

scholarly journals First steps towards time-resolved 'in-house' X-ray diffraction experiments

2014 ◽  
Vol 70 (a1) ◽  
pp. C775-C775 ◽  
Author(s):  
Radoslaw Kaminski ◽  
Jason Benedict ◽  
Elzbieta Trzop ◽  
Katarzyna Jarzembska ◽  
Bertrand Fournier ◽  
...  
Keyword(s):  
Excited State ◽  
Time Resolution ◽  
Structural Changes ◽  
Laser Pulses ◽  
High Repetition Rate ◽  
X Ray Diffraction ◽  
Laboratory Equipment ◽  
Time Resolved ◽  
X Ray ◽  
Ligand Charge Transfer

High-intensity X-ray sources, such as synchrotrons or X-ray free electron lasers, providing up to 100 ps time-resolution allow for studying very short-lived excited electronic states in molecular crystals. Some recent examples constitute investigations of Rh...Rh bond shortening,[1] or metal-to-ligand charge transfer processes in CuI complexes.[2] Nevertheless, in cases in which the lifetime of excited state species exceeds 10 μs it is now possible, due to the dramatic increase in the brightness of X-ray sources and the sensitivity of detectors, to use laboratory equipment to explore structural changes upon excitation. Consequently, in this contribution we present detailed technical description of the 'in-house' X-ray diffraction setup allowing for the laser-pump X-ray-probe experiments within the time-resolution at the order of 10 μs or larger. The experimental setup consists of a modified Bruker Mo-rotating-anode diffractometer, coupled with the high-frequency Nd:YAG laser (λ = 355 nm). The required synchronization of the laser pulses and the X-ray beam is realized via the optical chopper mounted across the beam-path. Chopper and laser capabilities enable high-repetition-rate experiments reaching up to 100 kHz. In addition, the laser shutter is being directly controlled though the original diffractometer software, allowing for collection of the data in a similar manner as done at the synchrotron (alternating light-ON & light-OFF frames). The laser beam itself is split into two allowing for improved uniform light delivery onto the crystal specimen. The designed setup was tested on the chosen set of crystals exhibiting rather long-lived excited state, such as, the Cu2Br2L2 (L = C5H4N-NMe2) complex, for which the determined lifetime is about 100 μs at 90 K. The results shall be presented. Research is funded by the National Science Foundation (CHE1213223). KNJ is supported by the Polish Ministry of Science and Higher Education through the "Mobility Plus" program.

scholarly journals Time-resolved X-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin.

1991 ◽  
Vol 10 (3) ◽  
pp. 521-526 ◽  
Author(s):  
M. H. Koch ◽  
N. A. Dencher ◽  
D. Oesterhelt ◽  
H. J. Plöhn ◽  
G. Rapp ◽  
...  
Keyword(s):  
Diffraction Study ◽  
Structural Changes ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray

scholarly journals Observation of Transient Structural Changes on Hydrogen Absorption Process of LaNi4.75Sn0.25 by Time Resolved X-Ray Diffraction

2015 ◽  
Vol 79 (3) ◽  
pp. 124-130 ◽  
Author(s):  
Akihiko Machida ◽  
Kensuke Higuchi ◽  
Yoshinori Katayama ◽  
Kouji Sakaki ◽  
Hyunjeong Kim ◽  
...  
Keyword(s):  
Hydrogen Absorption ◽  
Structural Changes ◽  
Absorption Process ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray

Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction

1986 ◽  
Vol 188 (3) ◽  
pp. 325-342 ◽  
Author(s):  
M. Kress ◽  
H.E. Huxley ◽  
A.R. Faruqi ◽  
J. Hendrix
Keyword(s):  
Structural Changes ◽  
Frog Muscle ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray

Ultrafast X-ray diffraction in liquid, solution and gas: present status and future prospects

2010 ◽  
Vol 66 (2) ◽  
pp. 270-280 ◽  
Author(s):  
Jeongho Kim ◽  
Kyung Hwan Kim ◽  
Jae Hyuk Lee ◽  
Hyotcherl Ihee
Keyword(s):  
Single Molecule ◽  
Reaction Dynamics ◽  
Liquid Solution ◽  
Substantial Improvement ◽  
Photon Flux ◽  
Solvation Dynamics ◽  
Structural Transitions ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray

In recent years, the time-resolved X-ray diffraction technique has been established as an excellent tool for studying reaction dynamics and protein structural transitions with the aid of 100 ps X-ray pulses generated from third-generation synchrotrons. The forthcoming advent of the X-ray free-electron laser (XFEL) will bring a substantial improvement in pulse duration, photon flux and coherence of X-ray pulses, making time-resolved X-ray diffraction even more powerful. This technical breakthrough is envisioned to revolutionize the field of reaction dynamics associated with time-resolved diffraction methods. Examples of candidates for the first femtosecond X-ray diffraction experiments using highly coherent sub-100 fs pulses generated from XFELs are presented in this paper. They include the chemical reactions of small molecules in the gas and solution phases, solvation dynamics and protein structural transitions. In these potential experiments, ultrafast reaction dynamics and motions of coherent rovibrational wave packets will be monitored in real time. In addition, high photon flux and coherence of XFEL-generated X-ray pulses give the prospect of single-molecule diffraction experiments.

scholarly journals Observation of the shock-induced β-Sn to b.c.t.-Sn transition using time-resolved X-ray diffraction

2019 ◽  
Vol 26 (1) ◽  
pp. 96-101 ◽  
Author(s):  
R. Briggs ◽  
R. Torchio ◽  
A. Sollier ◽  
F. Occelli ◽  
L. Videau ◽  
...  
Keyword(s):  
Phase Transition ◽  
European Synchrotron Radiation Facility ◽  
Maximum Pressure ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray ◽  
Reverse Transition ◽  
First Time ◽  
Pressure Phase ◽  
Good Agreement

Time-resolved X-ray diffraction measurements have been carried out on dynamically compressed Sn up to a maximum pressure of ∼13 GPa at the European Synchrotron Radiation Facility. The phase transition from β-Sn to body-centered tetragonal (b.c.t.) Sn has been observed using synchrotron X-ray diffraction for the first time undergoing shock compression and release. Following maximum compression, the sample releases to lower pressures for several nanoseconds until the reverse transition occurs. The data are in good agreement with previous shock boundaries that indicate that the β-Sn phase is stable ∼2 GPa higher than the static boundary upon compression and the b.c.t.-Sn phase is stable ∼1 GPa lower upon release. The transition to the high-pressure phase reveals a loss of texture in the X-ray diffraction data from the `quasi' single-crystal β-Sn structure to a more powder-like Debye–Scherrer ring.

scholarly journals 1P161 Time resolved X-ray diffraction studies of the structural changes of actosmooth S1 complex induced by the photolysis of caged ADP

2004 ◽  
Vol 44 (supplement) ◽  
pp. S70
Author(s):  
J. Wakayama ◽  
T. Tamura ◽  
K. Inoue ◽  
N. Yagi ◽  
H. Iwamoto
Keyword(s):  
Structural Changes ◽  
X Ray Diffraction ◽  
Time Resolved ◽  
X Ray

scholarly journals Effect of hydrothermal treatment on the structure of an aluminosilicate polymer

2013 ◽  
Vol 11 (5) ◽  
pp. 782-789 ◽  
Author(s):  
Jaroslav Melar ◽  
Vratislav Bednarik ◽  
Roman Slavik ◽  
Miroslav Pastorek
Keyword(s):  
Electron Microscopy ◽  
Hydrothermal Treatment ◽  
Structural Changes ◽  
Polycondensation Reaction ◽  
X Ray Diffraction ◽  
Microscopy Imaging ◽  
X Ray ◽  
Crystalline Product ◽  
Amorphous Aluminosilicate ◽  
Scanning Electron

AbstractThe effect of hydrothermal treatment on the structure of an aluminosilicate polymer prepared by a polycondensation reaction between silicate and hydroxoaluminate in alkaline aqueous solution was studied. The structural changes were investigated using X-ray diffraction analysis, Fourier-transform infrared spectroscopy, scanning electron microscopy imaging and thermogravimetric analysis. The results indicated that the amorphous aluminosilicate polymer transformed into a crystalline product during the hydrothermal treatment at 145°C. The crystalline phase was identified as a mineral of the zeolite group, most likely phillipsite. This transformation required an alkaline environment during the hydrothermal treatment.

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