scholarly journals Synchrotron X-ray footprinting on tour

2013 ◽  
Vol 21 (1) ◽  
pp. 24-31 ◽  
Author(s):  
Jen Bohon ◽  
Rhijuta D'Mello ◽  
Corie Ralston ◽  
Sayan Gupta ◽  
Mark R. Chance
Keyword(s):  
Structural Biology ◽  
Technology Development ◽  
Standard Sample ◽  
X Ray ◽  
Structure And Dynamics ◽  
The Usa ◽  
Synchrotron Light ◽  
General User ◽  
Single Facility ◽  
Macromolecular Solution

Synchrotron footprinting is a valuable technique in structural biology for understanding macromolecular solution-state structure and dynamics of proteins and nucleic acids. Although an extremely powerful tool, there is currently only a single facility in the USA, the X28C beamline at the National Synchrotron Light Source (NSLS), dedicated to providing infrastructure, technology development and support for these studies. The high flux density of the focused white beam and variety of specialized exposure environments available at X28C enables footprinting of highly complex biological systems; however, it is likely that a significant fraction of interesting experiments could be performed at unspecialized facilities. In an effort to investigate the viability of a beamline-flexible footprinting program, a standard sample was taken on tour around the nation to be exposed at several US synchrotrons. This work describes how a relatively simple and transportable apparatus can allow beamlines at the NSLS, CHESS, APS and ALS to be used for synchrotron footprinting in a general user mode that can provide useful results.

scholarly journals The XFP (17-BM) beamline for X-ray footprinting at NSLS-II

2019 ◽  
Vol 26 (4) ◽  
pp. 1388-1399 ◽  
Author(s):  
Awuri Asuru ◽  
Erik R. Farquhar ◽  
Michael Sullivan ◽  
Donald Abel ◽  
John Toomey ◽  
...  
Keyword(s):  
Structural Biology ◽  
Ring Current ◽  
Incident Power ◽  
Sample Handling ◽  
X Ray ◽  
Structure And Dynamics ◽  
State Technique ◽  
Incident Power Density ◽  
General User ◽  
Standard Protein

Hydroxyl-radical mediated synchrotron X-ray footprinting (XF) is a powerful solution-state technique in structural biology for the study of macromolecular structure and dynamics of proteins and nucleic acids, with several synchrotron resources available to serve the XF community worldwide. The XFP (Biological X-ray Footprinting) beamline at the NSLS-II was constructed on a three-pole wiggler source at 17-BM to serve as the premier beamline for performing this technique, providing an unparalleled combination of high flux density broadband beam, flexibility in beam morphology, and sample handling capabilities specifically designed for XF experiments. The details of beamline design, beam measurements, and science commissioning results for a standard protein using the two distinct XFP endstations are presented here. XFP took first light in 2016 and is now available for general user operations through peer-reviewed proposals. Currently, beam sizes from 450 µm × 120 µm to 2.7 mm × 2.7 mm (FWHM) are available, with a flux of 1.6 × 1016 photons s−1 (measured at 325 mA ring current) in a broadband (∼5–16 keV) beam. This flux is expected to rise to 2.5 × 1016 photons s−1 at the full NSLS-II design current of 500 mA, providing an incident power density of >500 W mm−2 at full focus.

Development of Synchrotron Footprinting at NSLS and NSLS-II

2019 ◽  
Vol 26 (1) ◽  
pp. 55-60 ◽  
Author(s):  
Jen Bohon
Keyword(s):  
Solvent Accessibility ◽  
Biological Systems ◽  
In Vivo Studies ◽  
Aqueous Samples ◽  
Biological Mechanisms ◽  
Macromolecular Assembly ◽  
Structure And Dynamics ◽  
Synchrotron Light ◽  
Ideal Technique

Background: First developed in the 1990’s at the National Synchrotron Light Source, xray synchrotron footprinting is an ideal technique for the analysis of solution-state structure and dynamics of macromolecules. Hydroxyl radicals generated in aqueous samples by intense x-ray beams serve as fine probes of solvent accessibility, rapidly and irreversibly reacting with solvent exposed residues to provide a “snapshot” of the sample state at the time of exposure. Over the last few decades, improvements in instrumentation to expand the technology have continuously pushed the boundaries of biological systems that can be studied using the technique. Conclusion: Dedicated synchrotron beamlines provide important resources for examining fundamental biological mechanisms of folding, ligand binding, catalysis, transcription, translation, and macromolecular assembly. The legacy of synchrotron footprinting at NSLS has led to significant improvement in our understanding of many biological systems, from identifying key structural components in enzymes and transporters to in vivo studies of ribosome assembly. This work continues at the XFP (17-BM) beamline at NSLS-II and facilities at ALS, which are currently accepting proposals for use.

scholarly journals Use of WetSEM® capsules for convenient multimodal scanning electron microscopy, energy dispersive X-ray analysis, and micro Raman spectroscopy characterisation of technetium oxides

2021 ◽  
Author(s):  
D. J. Bailey ◽  
M. C. Stennett ◽  
J. Heo ◽  
N. C. Hyatt
Keyword(s):  
Raman Spectroscopy ◽  
Low Cost ◽  
Powder Materials ◽  
Spectroscopy Analysis ◽  
X Ray ◽  
Micro Raman Spectroscopy ◽  
Hazard And Risk ◽  
Sem Imaging ◽  
General User ◽  
532 Nm

AbstractSEM–EDX and Raman spectroscopy analysis of radioactive compounds is often restricted to dedicated instrumentation, within radiological working areas, to manage the hazard and risk of contamination. Here, we demonstrate application of WetSEM® capsules for containment of technetium powder materials, enabling routine multimodal characterisation with general user instrumentation, outside of a controlled radiological working area. The electron transparent membrane of WetSEM® capsules enables SEM imaging of submicron non-conducting technetium powders and acquisition of Tc Lα X-ray emission, using a low cost desktop SEM–EDX system, as well as acquisition of good quality μ-Raman spectra using a 532 nm laser.

scholarly journals Local Structure and Dynamics of Functional Materials Studied by X-ray Absorption Fine Structure

Symmetry ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1315
Author(s):  
Takafumi Miyanaga
Keyword(s):  
Fine Structure ◽  
Local Structure ◽  
Chemical Reactivity ◽  
Functional Materials ◽  
X Ray ◽  
Structure And Dynamics ◽  
Absorption Fine ◽  
Structure Phase Transition ◽  
Local Electronic Structure ◽  
X Ray Absorption

X-ray absorption fine structure (XAFS) is a powerful technique used to analyze a local electronic structure, local atomic structure, and structural dynamics. In this review, I present examples of XAFS that apply to the local structure and dynamics of functional materials: (1) structure phase transition in perovskite PbTiO3 and magnetic FeRhPd alloys; (2) nano-scaled fluctuations related to their magnetic properties in Ni–Mn alloys and Fe/Cr thin films; and (3) the Debye–Waller factors related to the chemical reactivity for catalysis in polyanions and ligand exchange reaction. This study shows that the local structure and dynamics are related to the characteristic function of the materials.

scholarly journals XRD Data Visualization, Processing and Analysis with d1Dplot and d2Dplot Software Packages

Proceedings ◽  
2020 ◽  
Vol 62 (1) ◽  
pp. 9
Author(s):  
Oriol Vallcorba ◽  
Jordi Rius
Keyword(s):  
Data Analysis ◽  
Data Visualization ◽  
X Ray Diffraction ◽  
Specific Data ◽  
X Ray ◽  
Software Packages ◽  
Compound Database ◽  
Synchrotron Light ◽  
User Friendly ◽  
Transformation Processes

The d1Dplot and d2Dplot computer programs have been developed as user-friendly tools for the inspection and processing of 1D and 2D X-ray diffraction (XRD) data, respectively. d1Dplot provides general tools for data processing and includes the ability to generate comprehensive 2D plots of multiple patterns to easily follow transformation processes. d2Dplot is a full package for 2D XRD data. Besides general processing tools, it includes specific data analysis routines for the application of the through-the-substrate methodology [Rius et al. IUCrJ 2015, 2, 452–463]. Both programs allow the creation of a user compound database for the identification of crystalline phases. The software can be downloaded from the ALBA Synchrotron Light Source website and can be used free of charge for non-commercial and academic purposes.

scholarly journals Technology development of the soft X-ray tomography system in Wendelstein 7-X stellarator

2013 ◽  
Vol 88 (9-10) ◽  
pp. 1987-1991 ◽  
Author(s):  
M. Schülke ◽  
A. Cardella ◽  
D. Hathiramani ◽  
S. Mettchen ◽  
H. Thomsen ◽  
...  
Keyword(s):  
Technology Development ◽  
X Ray ◽  
Tomography System

Structure and dynamics of 1,4-dioxane-water binary solutions studied by X-ray diffraction, mass spectrometry, and NMR relaxation

1999 ◽  
Vol 83 (1-3) ◽  
pp. 163-177 ◽  
Author(s):  
Toshiyuki Takamuku ◽  
Atsushi Yamaguchi ◽  
Masaaki Tabata ◽  
Nobuyuki Nishi ◽  
Koji Yoshida ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Nmr Relaxation ◽  
X Ray Diffraction ◽  
Binary Solutions ◽  
X Ray ◽  
Structure And Dynamics

Development of Diamond-Based X-ray Detection for High Flux Beamline Diagnostics

2009 ◽  
Vol 1203 ◽  
Author(s):  
Jen Bohon ◽  
John Smedley ◽  
Erik M. Muller ◽  
Jeffrey W. Keister
Keyword(s):  
Single Crystal ◽  
Linear Response ◽  
Voltage Dependence ◽  
Cvd Diamond ◽  
High Flux ◽  
National Synchrotron Light Source ◽  
X Ray ◽  
Single Crystal Diamond ◽  
Synchrotron Light ◽  
Pulse Structure

AbstractHigh quality single crystal and polycrystalline CVD diamond detectors with platinum contacts have been tested at the white beam X28C beamline at the National Synchrotron Light Source under high-flux conditions. The voltage dependence of these devices has been measured under DC and pulsed-bias conditions, establishing the presence or absence of photoconductive gain in each device. Linear response has been achieved over eleven orders of magnitude when combined with previous low flux studies. Temporal measurements with single crystal diamond detectors have resolved the ns scale pulse structure of the NSLS.

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