A SAXSess (Anton Paar, Austria) SAXS and WAXS camera was used to analyze the prepared samples. The X-rays (Cu Kα, λ＝0.1542 nm) employed to irradiate the samples were generated utilizing a sealed glass X-ray tube and were collimated using a block optical system. A glass capillary sample cell (sample thickness of 1 mm) was used as sample cell, and the scattered X-rays were detected using an image plate. The image plate was analyzed using a Cyclone (Perkin Elmer, USA) imager, and the one-dimensional spectra of the samples were obtained using the SAX-Squant (Anton Paar, Austria) software. The measurements were performed at the X-ray generator voltage and current of 40 kV and 50 mA, respectively, and at the X-ray irradiation time of 10 min.
Saxsquant
Manufactured by Anton Paar
Sourced in Austria
SAXSQuant is a laboratory equipment designed for small-angle X-ray scattering (SAXS) analysis. It is used to obtain information about the size, shape, and structure of nanoscale and mesoscale materials. The device measures the intensity of X-rays scattered at small angles, providing data that can be used to determine the characteristics of the analyzed sample.
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Lab products found in correlation
5 protocols using saxsquant
1
Small-Angle X-Ray Scattering Protocol
2
Structural Ensemble Determination of PKA-C/PKIα Complex
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SAXS data were collected at the University of Utah using an Anton Paar SAXess instrument with line collimation and solid-state detector. In both PKIα free and the PKA-C/PKIα complex, the proteins were equilibrated by dialysis in buffer containing 20 mM MOPS, 90 mM KCl, 60 mM MgCl2, 10 mM DTT, 1 mM NaN3 (pH 6.5), and 12 mM of ATPγN. For measurements of the PKIα free form, a protein concentration of 1 mM was used, and for the PKA-C/PKIα complex sample, a final protein concentration 0.2 mM protein with PKA-C/PKIα in 1:1 molar ratio. SAXS data were reduced and desmeared using the SAXSQuant (Anton Paar) software suite and further analyzed using PRIMUS in the ATSAS 2.8.3 software suite (Franke et al., 2017 (link)). The fitting of the MD structural ensembles to the experimental scattering data was performed using the MultiFoXS server (Schneidman-Duhovny et al., 2013 (link)). 100 random snapshots from MD simulations with different radius of gyration (Rg) were chosen as the conformational ensembles, and the fitting was done for the q range (0.01 to approximately 0.18 Å−1). The top 10 structures with the lowest χ values were selected as the final structure ensembles.
3
Analysis of Lamellar Structure in Dried Creams
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The dried films of the test and control creams were evaluated using a small- and wide-angle X-ray scattering apparatus (SAXSess mc2; Anton Paar GmbH, Graz, Austria). For sampling of the dried film, the substance was applied on a polyethylene terephthalate resin overhead projector film with a coater (120 μm thickness), dried for 3 h, scraped with a spatula, and placed into cells. Paste cells specific for SAXSess mc2 were used as sample cells. X-Ray scatter detection was performed using an imaging plate for SAXSess mc2. The measurement conditions were as follows: X-ray wavelength, 0.1542 nm; sample–detector distance, 259.2 mm; and measurement temperature, 25 °C. The exposure time was set at 5–60 min on the basis of the balance between the irradiation limit of the Imagine Plate and detection sensitivity (signal-to-noise ratio). After exposure to the imaging plate, on the basis of the acquired two-dimensional scattering images, a one-dimensional scattering profile was created using the accessory software provided with SAXSess mc2 (SAXSquant 2D; SAXSquant, Anton Paar GmbH). The period d [nm] of the lamellar structure observed on X-ray scattering was determined from the peak position as follows: q = 2π/d [nm−1], where q is the scattering vector.
4
SAXS Analysis of TMAT-AuNPs
5
Comprehensive Material Characterization Protocol
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Analysis of variance, through Tukey’s mean comparison test (p < 0.05), was performed in Prism 9 (GraphPad Software, Inc., San Diego, CA, USA). Rheology device control and the calculation of rheological parameters were performed under TRIOS Software, Version 4.1.1.33073 (TA Instruments, New Castle, DE, USA). The SAXSquant and SAXSquant2D software package (Anton Paar GmbH, Graz, Austria) were used to control the SAXS device, the data acquisition, and the normalization of the SAXS profile masks after profile integration. X’Pert HighScore Plus software (PANanalytical, Almelo, The Netherlands) was used to gather XRD data, collected at 174 s, and to perform peak diffractions analysis. Hardness was calculated using the Texture Exponent v.6.1.1.0 software (Stable Microsystems, Godalming, UK).
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