The Xeuss SAXS/WAXS system (Xenocs, Sassenage, France) features a 30 W Cu Kα microfocus tube with ultra low divergence mirror optics (GeniX, Sassenage, France) and a Pilatus 300 K/20 Hz hybrid pixel detector (DECTRIS, Baden Dättwil, Switzerland). Focus area at the sample is 0.6 mm² for high resolution collimation. The motorized components were controlled with SPEC software. The samples were filled into a Kapton flow-through capillary (inner diameter 1 mm, wall thickness ± 0.025 mm (Goodfellow GmbH, Germany)) mounted on a Linkam stage (Linkam Scientific Instruments, United Kingdom) kept at room temperature. The sample-to-detector distance for SAXS was 2770 mm, calibrated with silver behenate. The absolute calibration of the scattering data was done with glassy carbon type 2, sample P11116 (link). The X-ray scattering vector q is defined as q = 4π/λ sin(θ) at a scattering angle of 2θ. Data were fitted by several model functions for smooth hard spheres, fuzzy spheres and hard spheres decorated with a layer of Gaussian chains117 (link). Only the latter fit function was able to describe the data over the full range of scattering vectors down to the noise level.
Pilatus 300 k 20 hz hybrid pixel detector
Manufactured by Dectris
Sourced in France
The Pilatus 300 K/20 Hz hybrid pixel detector is a high-performance X-ray detector designed for a variety of scientific applications. It features a large active area, high frame rate, and low noise, making it suitable for advanced research and analysis tasks.
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Lab products found in correlation
3 protocols using pilatus 300 k 20 hz hybrid pixel detector
1
Small-Angle X-Ray Scattering of Nanostructures
2
Lipid Film Adsorption and Characterization
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Lipid films were adsorbed onto the pre-stretched PDMS substrates (1.2 × 1.2 cm2). Approximately 100 μL of the stock solution of lipids (20 mM) in ethanol was drop-casted onto the substrate and allowed to dry in air. Later, the samples were dried-vacuum for at least two hours and the samples were incubated at 50 °C in high relative humidity (RH ≈ 95%) for 4 hours. Finally, the pre-stretched samples were released before characterization. To characterize the lipid film structure and orientation, GISAXS/GIWAXS was conducted in a custom built (with Forvis Technologies, Santa Barbara) equipment composed of a Xenocs GeniX3D Cu κα ultralow divergence X-ray source (1.54 Å/8 keV), with a divergence of 1.3 mrad. Multiple measurements were carried on the same sample in the uncompressed and compressed states, varying the incidence angle to determine the most appropriate operating angle. The sample-to-detector distance was calibrated using a silver behenate powder standard. The 2D diffraction data were radially averaged upon acquisition on a Pilatus 300 K 20 Hz hybrid pixel detector (Dectris). The 2D diffraction patterns were reduced to 1D plots using SAS2D [72 (link)].
3
SAXS Analysis of Gliadin Protein
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SAXS of gliadin was performed on a Xeuss SAXS/WAXS System (Xenocs, Sassenage, France).
The X-ray source consists of a 30 W CuK α (λ=1.54 Å) microfocus tube with an ultra-low divergence mirror optics (GeniX, Sassenage, France) and a Pilatus 300K, 20 Hz hybrid pixel detector (DECTRIS, Baden-Deatwil, Switzerland). The scattering curves were normalised by the integrated intensity incident on the sample, exposure time, sample thickness, transmission and background. The focus of the sample was 1 mm². The samples were measured in a 1 mm flowthrough Kapton capillary (Goodfellow GmbH, Bad Nauheim, Germany) placed in a Linkam stage (Linkam Scientific, Tadworth, UK) at 10 °C. The sample-to-detector distance was for SAXS 2772 mm, calibrated with silver behenate. The range of the scattering vector was around q=0.7 -0.13 nm -1 at a scattering angle of 2θ. The absolute calibration of the scattering data was done with glassy carbon type 2 [11] . The scattered intensity I(q)=N•I(0)•(Δρ) 2 •V 2 •P(q) •S(q) is dependent on: the incident intensity I(0), the scattering volume of the colloid V, the electron density difference Δρ between particle and solvent and the particle form factor P(q). The particle structure factor S(q) equals to one for dilute systems.
The X-ray source consists of a 30 W CuK α (λ=1.54 Å) microfocus tube with an ultra-low divergence mirror optics (GeniX, Sassenage, France) and a Pilatus 300K, 20 Hz hybrid pixel detector (DECTRIS, Baden-Deatwil, Switzerland). The scattering curves were normalised by the integrated intensity incident on the sample, exposure time, sample thickness, transmission and background. The focus of the sample was 1 mm². The samples were measured in a 1 mm flowthrough Kapton capillary (Goodfellow GmbH, Bad Nauheim, Germany) placed in a Linkam stage (Linkam Scientific, Tadworth, UK) at 10 °C. The sample-to-detector distance was for SAXS 2772 mm, calibrated with silver behenate. The range of the scattering vector was around q=0.7 -0.13 nm -1 at a scattering angle of 2θ. The absolute calibration of the scattering data was done with glassy carbon type 2 [11] . The scattered intensity I(q)=N•I(0)•(Δρ) 2 •V 2 •P(q) •S(q) is dependent on: the incident intensity I(0), the scattering volume of the colloid V, the electron density difference Δρ between particle and solvent and the particle form factor P(q). The particle structure factor S(q) equals to one for dilute systems.
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