Genix

Manufactured by Xenocs

Sourced in Switzerland

The GeniX is a high-performance X-ray source developed by Xenocs. It is designed to provide a stable and intense X-ray beam for various analytical techniques. The core function of the GeniX is to generate X-rays that can be used for sample analysis and characterization. The technical specifications and capabilities of the GeniX are available upon request.

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Lab products found in correlation

Pilatus 300k detector, by Dectris (4 mentions) Matlab, by MathWorks (3 mentions) Pilatus 300k, by Dectris (1 mentions)

6 protocols using genix

Aligned Amino Acid Nanostructure Characterization

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The amino acids were dissolved
in deionized water at a concentration of 2 mg/mL for individual amino
acids or 1 mg/mL each for dl-composites by heating to 90
°C. The assembled structures were drop-cast over a thin Kapton
film and left to dry in the presence of a magnetic field to produce
aligned structures. WAXS measurements were performed using an in-house
X-ray scattering system, with a GeniX (Xenocs) low-divergence Cu Kα
radiation source (wavelength of 1.54 Å) and a scatterless slits
setup.^{71 (link)} Two-dimensional scattering data,
with a momentum transfer wave vector (q) range of
0.07–2.5 Å^–1 at a sample-to-detector
distance of approximately 160 mm, were collected on a Pilatus 300
K detector (Dectris, Baden-Daettwil, Switzerland) and radially integrated
using Matlab (MathWorks, Natick, MA, USA)-based procedures (SAXSi).
Calibration was performed using silver behenate. The scattering data
of the empty Kapton film was collected as background and subtracted
from the sample measurement.

Bera S., Xue B., Rehak P., Jacoby G., Ji W., Shimon L.J., Beck R., Král P., Cao Y, & Gazit E. (2020). Self-Assembly of Aromatic Amino Acid Enantiomers into Supramolecular Materials of High Rigidity. ACS Nano, 14(2), 1694-1706.

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WAXS Analysis of SHR-FLLF Peptide Solutions

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The SHR-FLLF peptide solutions at a concentration of 15 and 5 mg ml⁻¹ were sealed in quartz capillaries with a 1.5 mm diameter. WAXS measurements were performed using an in-house X-ray scattering system, with a GeniX (Xenocs) low divergence Cu Kα radiation source (wavelength of 1.54 Å) and a scatterless slits setup48 . Two-dimensional scattering data, with a momentum transfer wave vector (q) range of 0.07−2.5 Å⁻¹ at a sample-to-detector distance of about 160 mm, was collected on a Pilatus 300 K detector (Dectris, Baden-Daettwil, Switzerland) and radially integrated using Matlab (MathWorks, Natick, MA, USA)-based procedures (SAXSi). Calibration was performed using silver behenate. The scattering data of the water at pH 2 was collected as background and used to subtract the solvent and spurious scattering from the WAXS system itself, for example, Kapton vacuum windows and air gaps.

Mondal S., Varenik M., Bloch D.N., Atsmon-Raz Y., Jacoby G., Adler-Abramovich L., Shimon L.J., Beck R., Miller Y., Regev O, & Gazit E. (2017). A minimal length rigid helical peptide motif allows rational design of modular surfactants. Nature Communications, 8, 14018.

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X-ray Scattering Protocol with Detailed Instrumentation

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Measurements were performed using a lab-based X-ray scattering system, with a GeniX (Xenocs) low divergence Cu

K_{α}

radiation source (wavelength of

λ = 1.54

Å) and a scatterless slits setup^{17 (link)}. The full-width-half-maximum of the direct beam is 1 mm in diameter, and the measured divergence is 0.0372 degrees (

2 θ

). Samples were measured at distance of

d_{s} = 117 mm

using Pilatus 300K detector (Dectris) having pixel size of

172 \times 172 μ m^{2}

(Ref.^{25 (link)}). The detector, sample stage, and slits were motorized using stepper motors with a positioning accuracy of 1

μ m

and controlled by SPEC software. In all the measured images, only valid pixels are used. We removed the gaps between the separate detector’s modules in pre-processing. All 2D images presented below were cropped to show the scattering on a single module. The measured flux for the different beam sizes is presented in the supplementary materials Section 2.

Gutman B., Mrejen M., Shabat G., Avinery R., Shkolnisky Y, & Beck R. (2020). Angular super-resolution retrieval in small-angle X-ray scattering. Scientific Reports, 10, 16038.

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Small-Angle X-ray Scattering of Glycolipid Samples

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The aggregated
GlcCer samples at 30 mg/mL concentration were measured in 1.5 mm diameter
sealed quartz capillaries. WAXS/SAXS measurements were performed using
an in-house solution X-ray scattering system, with a GeniX (Xenocs)
low divergence Cu K_α radiation source (wavelength
of 1.54 Å) and a scatterless slits setup.^{70 (link)} Two-dimensional scattering data with a wave vector amplitude
(Q) range of 0.06–2 Å^–1 at a sample-to-detector distance of about 230 mm were collected
on a Pilatus 300 K detector (Dectris), and radially integrated using
MATLAB (MathWorks) based procedures (SAXSi). Background scattering
data were collected from buffer solution alone. The background-subtracted
scattering correlation peaks were fitted using a Gaussian with a linearly
sloped baseline. For each sample, time-resolved correlation peaks
position, intensity, and width were extracted.

Paul A., Jacoby G., Laor Bar-Yosef D., Beck R., Gazit E, & Segal D. (2021). Glucosylceramide Associated with Gaucher Disease Forms Amyloid-like Twisted Ribbon Fibrils That Induce α-Synuclein Aggregation. ACS Nano, 15(7), 11854-11868.

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X-Ray Scattering Protocol for Lipid Samples

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Samples at 30 mg/ml lipid concentration were measured in 1.5 mm diameter sealed quartz capillaries. Measurements were performed using an in-house solution X-Ray scattering system, with a GeniX (Xenocs) low divergence Cu K α radiation source (wave length of 1.54 Å) and a scatter-less slits setup [19] . Two-dimensional scattering data with a q range of 0.06 -2 Å -1 at a sample-to-detector distance of about 230 mm were collected on a Pilatus 300K detector (Dectris), and radially integrated using MATLAB (MathWorks) based procedures (SAXSi). Background scattering data was collected from buffer solution alone. The background-subtracted scattering correlation peaks were fitted using a Gaussian with a linearly sloped baseline. For each sample, time-resolved correlation peaks position, intensity and width were extracted.

Jacoby G., Portnaya I., Danino D., Diamant H, & Beck R. (2020). Delayed nucleation in lipid particles. Soft matter, 16(1).

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Structural Analysis of NF Hydrogels

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The powder diffraction scattering data from NF hydrogels contained in quartz capillaries was integrated azimuthally and the intensity was plotted versus reciprocal distance q. The intensity, in arbitrary units, showed a broad peak with a maximum in the range of q = 0.1-0.2 nm À1 (see ref. 24 and 30). The peak location relates to the inter-filament spacing (d = 2p/q). Broadening of this peak is observed due to density fluctuations and the semi-flexible nature of the individual filaments. Baseline background of the form AÁq ÀB + C with B = 2-3 is subtracted (Fig. S2,ESI †), and the resultant peak is fitted with a Lorentzian function using Matlab routines. 13, 30 Preliminary experiments were performed at our home-lab using a Pilatus 300K detector and a Xenocs GeniX Low Divergence CuKa radiation source setup with scatterless slits. 31 Subsequent measurements were performed at synchrotron facilities: P12 beamline in DESY, Hamburg; SWING beamline in SOLEIL, Paris; and I911 SAXS beamline in MAX-lab, Lund with 10 keV.

Kornreich M., Malka-Gibor E., Laser-Azogui A., Doron O., Herrmann H, & Beck R. (2015). Composite bottlebrush mechanics: α-internexin fine-tunes neurofilament network properties. Soft matter, 11(29).

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