saxs detector eiger2 4m  (Dectris AG)

Journal: bioRxiv

Article Title: Combination of 3D and 2D small and wide angle X-ray scattering imaging reveals diminished bone quality in the superior human femoral neck cortex

doi: 10.64898/2026.03.03.709216

Figure Lengend Snippet: a)Schematic of the human femoral neck showing the superior and inferior anatomical regions, alongwith the locations from which thin sections and micropillars were extracted. b) Schematic representation of bone ultrastructure, showing the hierarchical organization and the relative scale of the imaging voxel (25× 25 ×25 µm 3 ). c)Typical 3D RSM, displaying the 4 analyzed scattering signals relating to the MCF organization: collagen equatorial scattering (1), collagen meridional scattering (2), mineral platelet thickness scattering (3), HA (002) diffraction (4). The blue arrow indicates the main MCF direction. d) Scattering intensity along the three orthogonal directions relative to the MCF orientation, indicated by the arrows in (c), plotted across the SAXS and WAXS regimes. e) Schematic representation of SASTT (i) and 2D scanning SAXS/WAXS (ii) experimental setups and location of scattering signal (4) on WAXS (only avaliable in the 2D experiment) detector. f) SAXS detector with location of scattering signals (1-3), and plot of scattering intensity in function of the azimuthal angle ϕ in the scattering range (3), indicated by the shaded ring. The mean intensity ( a 0 ), 2D degree of orientation ( a 1 /a 0 ) and orientation (Φ) of the scattering signal are indicated.

Article Snippet: The samples were raster scanned with a step size of 25 ×25 μm 2 over a 5× 5 mm 2 area in the central part of each quadrant with an exposure time of 0.1 s at each point, and the scattered X-rays were collected on X-Spectrum Lambda 3M (WAXS) and Dectris EIGER2 X 4M (SAXS) detectors placed 0.134 m and 6.9 m downstream of the samples respectively.

Techniques: Imaging

Journal: Protein Science : A Publication of the Protein Society

Article Title: Lipid exchange of apolipoprotein A‐I amyloidogenic variants in reconstituted high‐density lipoprotein with artificial membranes

doi: 10.1002/pro.4987

Figure Lengend Snippet: SAXS profiles including best fits obtained by using a core‐shell‐bicelle‐elliptical‐belt‐rough model for POPC rHDL WT (a), POPC rHDL L174S (c), DMPC rHDL WT (b), and DMPC rHDL L174S (d) at 37°C. DMPC, 1,2‐dimyristoyl‐d 54 ‐3‐sn‐glycerophosphatidylcholine; POPC, 1‐palmitoyl‐oleoyl‐d 64 ‐3‐sn‐glycerophosphatidylcholine; rHDL, reconstituted high‐density lipoprotein; SAXS, small‐angle x‐ray scattering; WT, wild‐type.

Article Snippet: The scattered intensity was recorded at room temperature (22 ± 1°C), with 1 Å wavelength x‐rays, using an Eiger2 4M SAXS detector (Dectris) within an evacuated flight tube.

Techniques:

Journal: Protein Science : A Publication of the Protein Society

Article Title: Lipid exchange of apolipoprotein A‐I amyloidogenic variants in reconstituted high‐density lipoprotein with artificial membranes

doi: 10.1002/pro.4987

Figure Lengend Snippet: Structural features of the POPC and DMPC nanodiscs containing WT or L174S ApoA‐I proteins. (a) Schematic representation of the model used in SASview to fit the SAXS data. (b, d, e, and g) Parameters obtained from the best‐fit curves are shown in Figure . Table in Data provide all the parameters obtained after fitting. (c and f) Calculated values. ApoA‐I, apolipoprotein A‐I; DMPC, 1,2‐dimyristoyl‐d 54 ‐3‐sn‐glycerophosphatidylcholine; POPC, 1‐palmitoyl‐oleoyl‐d 64 ‐3‐sn‐glycerophosphatidylcholine; SAXS, small‐angle x‐ray scattering.

Article Snippet: The scattered intensity was recorded at room temperature (22 ± 1°C), with 1 Å wavelength x‐rays, using an Eiger2 4M SAXS detector (Dectris) within an evacuated flight tube.

Techniques: