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Dxr2 raman spectrometer

Manufactured by Thermo Fisher Scientific
Sourced in United States

The DXR2 Raman spectrometer is a compact, high-performance instrument designed for a range of analytical applications. It utilizes Raman spectroscopy, a technique that provides detailed information about the molecular structure and composition of samples. The DXR2 is capable of analyzing a variety of materials, including solids, liquids, and powders, without the need for complex sample preparation.

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8 protocols using dxr2 raman spectrometer

1

Multimodal Characterization of Materials

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XRD data were collected using a PANalytical
Empyrean X-ray powder diffractometer equipped with a Bragg–Brentano
HD mirror and operated at 45 kV and 40 mA using Cu Kα radiation.
The scans were collected in the 2θ range of 15–90°
(step size, 0.033° and time per step, 3.2 s). Raman spectra were
collected with a Thermo Scientific DXR2 Raman spectrometer equipped
with a 532 nm laser using a spot size of 1.8 μm. The spectra
were acquired in the range of 100–3,500 cm–1 with a spectral resolution of 0.964 cm–1. Five
measurements at different locations of the sample with a measurement
time of 100 s were acquired and averaged. FTIR spectroscopy experiments
were performed on self-supporting pellets using a Bruker Alpha II
spectrometer in transmission mode (12 scans, 2 cm–1 resolution) under a N2 atmosphere. TEM measurements were
acquired with a FEI Talos F200X electron microscope operated at 200
kV. BET (Brunauer–Emmett–Teller) surface areas of the
materials were measured from the N2 physisorption isotherms
recorded at 77 K on an Anton Paar Nova 800 apparatus. The samples
were degassed at 300 °C under vacuum (10–3 mbar) for 3
h prior to measurement.
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2

Raman Spectroscopy Analysis of Biomaterials

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The chemical structures of synthetic HAP, Type I collagen standard, RBC, MRB and RBAS were recorded on a DXR2 Raman spectrometer (Thermo Fisher, Waltham, MA, USA) equipped with a 785 nm laser source, a grating of 400 lines mm−1 and an energy of 15.0 mW; the spectra were collected in the wavenumber range of 3100 to 350 cm−1, and all the samples were exposed 40 times for 5 s [2 (link)]. After scanning, the Raman data were baseline corrected, and phenylalanine (1003 ± 1 cm−1) was used as the normalization factor [29 (link)]; peak fitting was performed to analyze the content of the secondary structure component of the protein finally, which were all carried out by Origin (2021, Origin-Lab, Northampton, NC, USA).
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3

Raman Spectroscopy of Materials

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Raman spectroscopy measurements were performed on a DXR 2 Raman spectrometer (Thermo Fisher) using a 532 nm excitation laser with a spot size of ∼2.1 μm at an optical magnification of 10×. All measurements were carried out in the range of 106–3500 cm−1 using a full range grating with a resolution of 1200 lines mm−1. For each sample, at least five different areas of the sample were measured and averaged. In situ Raman spectroscopy measurements were conducted with the same instrument using a high temperature Linkam CCR1000 cell in which the sample was placed and exposed to N2 or CO2.
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4

Nanostructure Characterization of Electrodes

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A Zeiss Ultra 55 Field Emission Scanning Electron Microscope (FESEM) and a JEOL JSM-6480LV SEM were used for the study of the electrodes’ nanostructure. X-ray Photoelectron spectroscopy was performed on samples as received and after 60–480 seconds of Argon-ion etching at 4KV (0.7 μA of current) using an Oxford AXIS ULTRA instrument. Raman spectrum of the DLEG sample for confirming the formation of graphene from the polyimide during the engraving process was obtained by using a DXR2 Raman spectrometer from Thermo Scientific with a laser power of 5 mW, at a laser excitation of 514.5 nm, and 2 seconds of integration time. Energy-Dispersive X-ray Spectroscopy (EDS) of the sensor was implemented by using X-Mass from Oxford Instruments. No additional processing steps were performed on the sensors before the characterizations.
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5

Raman Spectroscopy Characterization Protocol

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Raman spectroscopy was performed on a DXR 2 Raman spectrometer (Thermo Fisher) equipped with a 532 nm excitation laser with a spot size of 2.1 μm. All ex situ measurements were performed in air at atmospheric pressure using a laser power in the range 2–5 mW. Four to six measurements at different locations of the sample with a measurement time ranging between 5–20 s were acquired and averaged. For in situ Raman measurements, a high-temperature Linkam CCR1000 cell was used. For the carbonaceous template removal, the sample was heated to 600 °C (heating rate of 10 °C min−1) under 50 ml min−1 of synthetic air. The temperature was held every 25 °C to collect Raman spectra.
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6

Raman Spectroscopic Analysis of 3D Printed Scaffolds

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Raman spectra analysis of the SCPP was conducted with a DXR2 Raman Spectrometer (ThermoFisher, Waltham, MA). SCPP crystals were transferred onto a disposable microscope slide (VWR, Radnor, PA) and placed in the instrument for analysis. The Raman Spectrometer was operated under the following conditions: A 528 nm laser, 0.1 mW of power, 25 μm slit aperture, and a 10× objective lens. The resulting spectrum was Raman shifted, baseline corrected, and smoothed.
The 3D printed scaffolds were crosslinked, washed with PBS, and were dried at 50 °C for 15 min prior to being placed on a disposable microscope slide. Once the scaffolds were placed in the Raman spectrometer, they were viewed under the Atlµs viewing mode with a 10× objective lens. The laser was focused on the region of interest and an image of the locale was captured. The Raman spectrometer was operated under the following conditions: a 528 nm laser, 0.3 mW of power, 25 μm slit aperture, and a 10× objective lens. Additionally, cell-laden scaffolds were placed under the Raman confocal microscope and imaged under a 10× objective lens.
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7

Protein Adsorption and Mechanical Properties of GO-Coated Silk Films

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The protein adsorption of P-GSF films with various GO contents was evaluated using bovine serum albumin (BSA) and fetal bovine serum protein (FBS), respectively, following the protocol of the BCA protein assay kit (Beyotime Biotechnology, Beijing, China). The mechanical properties of the films were determined by the tensile tests, in which the films were cut into strip shapes and the stretch speed was 0.1 mm/s. The respective surface topographies of GO-coated SF films (GSF), patterned SF films (P-SF), and GO-coated patterned SF films (P-GSF) were obtained by scanning electron microscope (SEM). Raman spectra and Raman scanning images of films were analyzed under a 532 nm laser irradiation by microscopic imaging Raman spectrometer (DXR2, Thermo Fisher Scientific, Waltham, MA, USA). The surface hydrophilicity of films was characterized by measurement of the water contact angle.
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8

Physico-chemical Characterization of Cellulose Esters

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Viscosity of pure [BMIM]HSO4 and [BMIM]HSO4/ethanol with different [BMIM]HSO4 mass concentration was measured by a Rheometer (MCR302, Anton Paar, Austria) under plate viscosity mode. Ultimate analysis of MCEL and PCEL was analyzed by an elemental analyzer (Vario Macro Cube Elementar, Germany). FTIR spectra was scanned by a Fourier transform infrared spectrometer (ALPHA, German Brucker, German) with a wave number of 4000–400 cm−1 under ATR mode. Raman spectrometer (DXR-2, Thermo Fisher Scientific, U.S.) was used to character the structure of MCEL and PCEL with a wave number of 3500–100 cm−1. The crystal form and crystal structure of MCEL and PCEL was established by X-ray power diffraction (XRD, Ultima IV, Rigaku UIV, Japan) using Cu radiation source (λ = 0.15406 nm) with operating voltage at 40 kV and 40 mA in scan range from 5° to 45° with a scan rate of 0.5° s−1 and step size 0.02°. The surface structures of MCEL and PCEL were scanned by a scanning electron microscope (SEM, VEGA, TESCAN, China) with accelerating voltage HV = 25.00 kV. Laser Particle Sizer (Jinan Winner Particle Instrument Co., LTD, China) was used to measure the particle size of MCEL and PCEL with sample concentration 10.4‰ in water, with testing range from 0.01–2000 μm.
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