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.
Saxsess mc2
Manufactured by Anton Paar
Sourced in Austria
The SAXSess mc2 is a small-angle X-ray scattering (SAXS) instrument developed by Anton Paar. It is designed to analyze the structure and properties of materials at the nanometer scale. The SAXSess mc2 can be used to characterize the size, shape, and distribution of nanoparticles, polymers, and other materials.
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Lab products found in correlation
Saxsquant 2d, by Anton Paar (2 mentions)
Pi scx 4300, by Teledyne (2 mentions)
Saxsquant, by Anton Paar (1 mentions)
S200 10 300 gl, by GE Healthcare (1 mentions)
Smartlab3, by Rigaku (1 mentions)
D8 discover diffractometer, by Bruker (1 mentions)
Dma q800, by TA Instruments (1 mentions)
Nicolet is10 ftir, by Thermo Fisher Scientific (1 mentions)
Pom bx51, by Olympus (1 mentions)
11 protocols using saxsess mc2
1
Analysis of Lamellar Structure in Dried Creams
2
Dry Coating Characterization by SAXS
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The small- and wide-angle X-ray scattering apparatus (SAXSess mc2, Anton Paar, Graz, Austria) was used to evaluate the dry coating produced by the test and control creams. To sample the dry coating, the test and control creams were applied to a PET resin overhead projector film using a coater (120 μm thickness), dried for 3 h at 22°C and 40% relative humidity (RH), and scratched off with a spatula before being transferred into the sample cell. For the sample cell, we used a paste cell dedicated for use with SAXSess mc2. An imaging plate dedicated for use with SAXSess mc2 was used as the detector for X-ray diffraction patterns. In terms of the conditions for measurement, the wavelength of the X-rays were λ = 0.1542 nm, sample-detector distance was set to 259.2 mm, and the measurement temperature was set to 25°C. The exposure time was set to between 5 and 60 minutes, depending on the balance between the irradiation limit of the imaging plate and detection sensitivity (SN ratio). The two-dimensional diffraction image obtained by exposing the imaging plate to light was used to create a one-dimensional diffraction profile using the SAXSess mc2-attached software (SAXSquant 2D, SAXSquant), (Anton Paar, Graz, Austria). Period d [nm] of the lamellar structure observed on X-ray scattering was determined from the peak position q = 2π/d [nm−1], where q is the scattering vector.
3
TRAP1 ADP-BeF Complex Characterization
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Protein samples were buffer exchanged via size-exclusion chromatography using S200 10/300 GL (GE Healthcare Life Sciences) prior to the experiment. 6 mg/mL of heterodimeric hTRAP1 (+/R402A) was incubated at 30˚C for 3 hr with 1 mM ADP-BeF in reaction buffer (20 mM potassium phosphate pH7.0, 50 mM KCl, 2 mM MgCl2, 1 mM DTT). After incubation, samples were spun down at 16,000xg for 10 min and transferred to a new tube. Each experiment was collected with a total of 90-min exposure (15 s x 360 frames) using an in-house (Anton Paar SAXSESS mc2, Graz, Austria) SAXS instrument. Fitting of scattering intensity was done using a custom-written software written in Python2.7 and Fortran (Elnatan, 2017 ; a copy is archived at https://github.com/elifesciences-publications/UCSFsaxs ). The software applies smearing correction accounting for slit-collimated geometry of the X-ray beam, and it uses a Bayesian algorithm to choose an optimal Dmax and smoothness of the P(r) (Hansen, 2000 (link)). The software also estimates protein molecular mass from an invariant, Qr (Rambo and Tainer, 2013 (link)).
4
Structural Analysis of Thin Films
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The crystalline structure of the films was studied by wide-angle X-ray diffraction (WAXD) with a D8 DISCOVER diffractometer (Bruker, Rheinstetten, Germany) using Cu-Kα radiation. Scattering angles varied from 5° to 40°. Small-angle X-ray scattering (SAXS) experiments were performed with “SAXSessmc2” (Anton Paar, Graz, Austria) and Rigaku SmartLab 3 (Rigaku Corporation, Tokyo, Japan) diffractometers.
5
Comprehensive Characterization of Liquid Crystal Elastomers
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A polarizing microscope (POM BX51, Olympus, Japan) was used to observe the director alignment and nematic state of polydomain and monodomain LCEs. Wide‐angle X‐ray scattering (SAXSess mc2, Anton Paar) was used for characterizing the alignment of LCE. The glass and nematic‐isotropic transition temperatures were measured using differential scanning calorimetry (DSC) on a Mettler‐Toledo calorimeter (DSC3, CH). The samples were first ramped up and then cooled down in the temperature range of −50 °C to 150 °C at a rate of 10 °C min−1 to eliminate the effect of thermal history on their phase transition; the ramp‐up and ramp‐down processes were then recorded in the same manner, and the data obtained were normalized for comparison. Thermogravimetry analysis (TGA, JING YI GAO KE) was used to obtain the decomposition temperatures with a heating rate of 10 °C min−1 and at a nitrogen (N2) flow rate of 100 mL min−1. The mechanical properties with rectangular LCE samples mounted on the clamp were measured using dynamic mechanical analysis (DMA Q800, TA Instruments, USA). Fourier Transform Infrared spectroscopy (FTIR Nicolet iS10, Thermo Fisher, USA) was used to detect hydrogen bonds at self‐healing truncated surface joints.
6
Structural Analysis of PVAHMs via SAXS
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To investigate the ordered structure of the PVAHMs, a small-angle X-ray scattering system (SAXS; Anton Paar SAXSess mc2, Graz, Austria; wavelength of 0.1542 nm, copper target, 40 kV, 50 mA) was employed. The film samples were installed on the membrane cell of the multifunctional sample stage. A blank cell was used to determine the background scattering. The sample and background scattering were measured for a certain period of time, and these measurements were used to normalize the intensity of the scattered beam.
7
Small-Angle X-Ray Scattering Characterization
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Small-angle X-ray scattering
experiment was performed on SAXSess mc2 (Anton Paar Gmbh,
Graz, Austria). The X-ray source used was a sealed copper tube (40
kV/50 mA; wavelength, 0.1542 nm), and the detector was an imaging
plate. Exposure time allotted was 30 min per scan.
experiment was performed on SAXSess mc2 (Anton Paar Gmbh,
Graz, Austria). The X-ray source used was a sealed copper tube (40
kV/50 mA; wavelength, 0.1542 nm), and the detector was an imaging
plate. Exposure time allotted was 30 min per scan.
8
SAXS Experimental Setup and Parameters
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The SAXS experiments were performed on SAXS ess mc2(Anton Paar, Austria); the incident X-ray wavelength was 1.54 Å; the distance from sample to detector was 1590 mm; the ambient temperature was 27 °C.
9
SAXS Characterization of Hsp90 Conformations
10
SAXS Analysis of hm-DNA-Bound Protein
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SAXS measurements were performed with Anton Paar SAXSess mc2 instrument with linecolimation and charge-coupled-device detection. The X-ray wavelength was 1.5418 Å (CuKα), the sample to detector was 306.8 mm and the sample slit width was 10 mm. Each sample was prepared in 300 μl solution contained 150 mM NaCl, 10 mM HEPES, pH=8.0, 5 mM DTT and 5% glycerol. For the hm-DNA-bound form, the protein was pre-incubated with hm-DNA (12-bp, upper strand: 5′-GGGCCmCGCAGGG-3′, mC=5-methyldeoxycytosine) at 1:1.2 molar ratio for 10 min on ice. To correct for interparticle interference, the data of protein sample were collected twice and each time for 1 h. The solution containing no protein sample was also tested as background.
The initial data were first processed using SAXSquant and the further analysis with ATSAS software. The SAXS data were only analysed these were collected in the first hour because there was no time effect on the samples. The radius of gyration Rg was estimated from primus. The distance distribution function P(r) was calculated in PCG package. The maximum particle dimension Dmax was estimated from the P(r) function as the r for which P(r)=0.
The initial data were first processed using SAXSquant and the further analysis with ATSAS software. The SAXS data were only analysed these were collected in the first hour because there was no time effect on the samples. The radius of gyration Rg was estimated from primus. The distance distribution function P(r) was calculated in PCG package. The maximum particle dimension Dmax was estimated from the P(r) function as the r for which P(r)=0.
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