Characterization of a back-illuminated CMOS camera for soft x-ray coherent scattering

A commercial scientific camera has been adapted and characterized at the SOLEIL Synchrotron with the aim to improve the acquisition capabilities on the soft X-ray coherent scattering experimental station at SEXTANTS beamline. This device is equipped by the last generation of back side illuminated scientific CMOS (BSI-sCMOS) of 2048 by 2048 pixels of 11 μm2 able to acquire low noise images with a frame rate up to 48 Hz. The camera's performance measurements have been done and shows a good level of readout noise, a large full-well capacity, a medium dark current and a good homogeneity, respectively, 1.6 e- rms (in High Gain mode), 80 000 e- (in Low Gain mode),<5 e-/pixel/s and ∼ 1%. The quantum efficiency (QE) measurement has been performed at the soft x-ray branch of the METROLOGIE beamline and gives a relatively good agreement with the expected theoretical values. Finally, the demonstration of the camera's efficiency and of the gain in useful time measurement related to the high frame rate have been performed with a series of Airy patterns images compared with an image recorded using the standard BSI-CDD already in operation at the SEXTANTS beamline

X-ray-induced radiophotodynamic therapy (RPDT) using lanthanide micelles: Beyond depth limitations

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Characterization of subnanometric layers by grazing incidence X-ray reflectometry

International audienceWe present a method to characterize subnanometric layers based on grazing incidence X-ray reflectometry. For this purpose, we propose to use a “Fabry–Pérot” type multilayer structure in order to improve the sensitivity of the measurement to the layer thickness. For our study, this structure consists of a thin layer of scandium inserted between two periodic chromium (Cr)/scandium (Sc) multilayers. We describe the principle and estimate the sensitivity of the method by simulation. Experiments were performed on two optimized Fabry–Pérot structures with 0.6 and 1.2 nm Sc layer thicknesses using a laboratory grazing incidence reflectometer at 8.048 keV (Cu Kα radiation). Fitting of experimental data allows determining the Sc layer thickness. Finally, the structural parameters used in the fit were confirmed by measurements at 3 keV on the hard X-ray branch of the synchrotron SOLEIL Metrology and Tests beamline

Development of fast, simultaneous and multi-technique scanning hard X-ray microscopy at Synchrotron Soleil

A distributed fast-acquisition system for synchronized multi-technique experiments is presented, in which the collection of metadata and the asynchronous merging of large data volumes from multiple detectors are managed as part of the data collection process. This fast continuous scanning scheme, named FLYSCAN, enables measurement of microscopy data on a timescale of milliseconds per pixel. Proof-of-principle multi-technique experiments, namely scanning X-ray fluorescence spectrometry combined with absorption, differential phase contrast and dark-field imaging, have been performed on biological and geological samples

Soft X-ray Radiation and Monte Carlo Simulations: Good Tools to Describe the Radiation Chemistry of Sub-keV Electrons

International audienceThe description of the biological effects of ionizing radiation requires a good knowledge of the dose deposition processes at both the cellular and molecular scales. However, experimental studies on the energy deposition specificity of sub-keV electrons, produced by most radiations, including high-energy photons and heavy ions, are scarce. Soft X-rays (0.2–2 keV) are here used to probe the physical and physico-chemical events occurring upon exposure of liquid water to sub-keV electrons. Liquid water samples were irradiated with a monochromatic photon beam at the SOLEIL synchrotron. Hydroxyl radical quantification was conducted through HO• scavenging using benzoate to form fluorescent hydroxybenzoate. The yields of HO• radicals exhibit a minimum around 1.5 keV, in good agreement with indirect observation. Moreover, they are relatively independent of the benzoate concentration in the range investigated, which corresponds to scavenging times of 170 ns to 170 ps. These results provide evidence that sub-keV electrons behave as high linear energy transfer particles, since they are able to deposit tens to hundreds of electronvolts in nanometric volumes

Study of XUV beam splitter flatness for use on a Michelson interferometer

International audienceA XUV Michelson interferometer has been developed by LIXAM/CEA/LCFIO and has been tested as a Fourier-transform spectrometer for measurement of X-ray laser line shape. The observed strong deformation of the interference fringes limited the interest of such an interferometer for plasma probing. Because the fringe deformation was coming from a distortion of the beam splitter (5 × 5 mm^2 open aperture, about 150 nm thick), several parameters of the multilayer deposition used for the beam splitter fabrication have been recently optimized. The flatness has been improved from 80 nm rms obtained by using the ion beam sputtering technique, to 20 nm rms by using the magnetron sputtering technique. Over 3 × 3 mm^2, the beam splitter has a flatness better than 4 nm rms

Probing the solution structure of Factor H using hydroxyl radical protein footprinting and cross-linking

International audienceThe control protein Factor H (FH) is a crucial regulator of the innate immune complement system, where it is active on host cell membranes and in the fluid phase. Mutations impairing the binding capacity of FH lead to severe autoimmune diseases. Here, we studied the solution structure of full-length FH, in its free state and bound to the C3b complement protein. To do so, we used two powerful techniques, hydroxyl radical protein footprinting (HRPF) and chemical cross-linking coupled with mass spectrometry (MS), to probe the structural rearrangements and to identify protein interfaces. The footprint of C3b on the FH surface matches existing crystal structures of C3b complexed with the N- and C-terminal fragments of FH. In addition, we revealed the position of the central portion of FH in the protein complex. Moreover, cross-linking studies confirmed the involvement of the C-terminus in the dimerization of FH