The hard X-ray beamline BL8 at the superconducting asymmetric wiggler at the 1.5 GeV Dortmund Electron Accelerator DELTA is described. This beamline is dedicated to X-ray studies in the spectral range from approximately 1 keV to approximately 25 keV photon energy. The monochromator as well as the other optical components of the beamline are optimized accordingly. The endstation comprises a six-axis diffractometer that is capable of carrying heavy loads related to non-ambient sample environments such as, for example, ultrahigh-vacuum systems, high-pressure cells or liquid-helium cryostats. X-ray absorption spectra from several reference compounds illustrate the performance. Besides transmission measurements, fluorescence detection for dilute sample systems as well as surface-sensitive reflection-mode experiments have been performed. The results show that high-quality EXAFS data can be obtained in the quick-scanning EXAFS mode within a few seconds of acquisition time, enabling time-resolved in situ experiments using standard beamline equipment that is permanently available. The performance of the new beamline, especially in terms of the photon flux and energy resolution, is competitive with other insertion-device beamlines worldwide, and several sophisticated experiments including surface-sensitive EXAFS experiments are feasible.
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http://dx.doi.org/10.1107/S0909049509000508 | DOI Listing |
Rev Sci Instrum
January 2025
Max Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr 45470, Germany.
X-ray spectroscopies are uniquely poised to describe the geometric and electronic structure of metalloenzyme active sites under a wide variety of sample conditions. UV/Vis (ultraviolet/visible) spectroscopy is a similarly well-established technique that can identify and quantify catalytic intermediates. The work described here reports the first simultaneous collection of full in situ UV/Vis and high-energy resolution fluorescence detected x-ray absorption spectra.
View Article and Find Full Text PDFACS Mater Lett
January 2025
Centre for Materials Science and Nanotechnology, Department of Chemistry, University of Oslo, PO Box 1033, Blindern 0315 Norway.
Whenever the cycling of Li-ion batteries is stopped, the electrode materials undergo a relaxation process, but the structural changes that occur during relaxation are not well-understood. We have used operando synchrotron X-ray diffraction with a time resolution of 1.24 s to observe the structural changes that occur when the lithiation of graphite and LiFePO electrodes are interrupted.
View Article and Find Full Text PDFCommun Chem
January 2025
ESRF - The European Synchrotron, 71 Avenue des Martyrs, Grenoble, France.
Serial macromolecular crystallography has become a powerful method to reveal room temperature structures of biological macromolecules and perform time-resolved studies. ID29, a flagship beamline of the ESRF 4th generation synchrotron, is the first synchrotron beamline in the world capable of delivering high brilliance microsecond X-ray pulses at high repetition rate for the structure determination of biological macromolecules at room temperature. The cardinal combination of microsecond exposure times, innovative beam characteristics and adaptable sample environment provides high quality complete data, even from an exceptionally small amount of crystalline material, enabling what we collectively term serial microsecond crystallography (SµX).
View Article and Find Full Text PDFPLoS Negl Trop Dis
January 2025
Department of Microbiology and Immunology, Faculty of Tropical Medicine, Mahidol University, Bangkok, Thailand.
Hemolysin co-regulated protein 1 (Hcp1) is a component of the cluster 1 Type VI secretion system (T6SS1) that plays a key role during the intracellular lifecycle of Burkholderia pseudomallei. Hcp1 is recognized as a promising target antigen for developing melioidosis diagnostics and vaccines. While the gene encoding Hcp1 is retained across B.
View Article and Find Full Text PDFAdv Mater
January 2025
School of Chemical Engineering, The University of Adelaide, Adelaide, SA, 5005, Australia.
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