HZSM-5 crystals were sprinkled on CaF2 windows and placed on the heated sample stage of an environmental Linkam FTIR600 cell (c.a. 50 mL internal volume) mounted on a (Bruker) Hyperion 3000 IR microscope coupled to a Vertex 80V FTIR at MIRIAM beamline B22 of Diamond Light Source. The infrared experiment requires only single crystals of the catalyst. To improve the sensitivity of the MS detection we typically added around 1 mg (up to 3 mg) of zeolite to the cell and checked that the spectra seen from one crystal were reproducibly seen from other crystals in the sample. The infrared experiments were collected in transmission from individual crystals at spatial resolution down to 10 × 10 micron at the sample using a 36× objective/condenser optics, averaging 16 scans at 4 cm -1 resolution, i.e. typically collecting an IR spectrum every two seconds. The output of the gas phase products from the cell was analysed by mass spectrometry (Pfeiffer or EcoSys) and correlated with the time-resolved IR spectral changes. Gases or liquids were introduced into a nitrogen flow (100 mL min -1 ) upstream of the heated cell at temperatures up to 673 K and ambient pressure. Multiple methanol pulses (each pulse 8 µL in volume) were syringe injected, and dimethylether (5 mL min -1 ) was diluted in the nitrogen stream and introduced in a continuous flow.
Hyperion 3000 ir microscope
Manufactured by Bruker
Sourced in Germany
The Hyperion 3000 IR microscope is a high-performance infrared imaging system designed for analytical applications. It provides non-destructive, label-free imaging and spectroscopic analysis of samples. The instrument features a high-resolution optical system, advanced detector technology, and user-friendly software for data acquisition and processing.
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Lab products found in correlation
Tensor 27 ir spectrometer, by Bruker (2 mentions)
Vertex 80 5 ftir, by Bruker (1 mentions)
80 v spectrometer, by Bruker (1 mentions)
Tensor 2 ftir spectrometer, by Bruker (1 mentions)
Ftir 600, by Linkam (1 mentions)
66 5 ftir spectrometer, by Bruker (1 mentions)
Vacuum ft ir vertex 70 5 spectrometer, by Bruker (1 mentions)
Opus software, by Bruker (1 mentions)
Vertex 80v ftir spectrometer, by Bruker (1 mentions)
Vertex70 ir spectrometer, by Bruker (1 mentions)
12 protocols using hyperion 3000 ir microscope
1
In situ Infrared Spectroscopy of Catalytic Reactions
2
Characterization of Imprinted Polymer Films
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The imprinted and reference polymer films were characterized with RAIRS measurements using a Bruker Hyperion 3000 IR microscope with a built-in Tensor 27 IR spectrometer and a computerized sample stage. The IR beam was surface reflected twice at the surface with a grazing angle objective at 52° and 83° to the surface normal. A mercury-cadmium-telluride (MCT) detector was utilized to collect 1000 interferograms at 4 cm-1 resolution. Prior to Fourier transformation, the interferograms were corrected using a three-term Blackmann–Harris apodization function. The sample chamber was purged with N2 to maintain an inert atmosphere throughout the measurement. An unmodified gold-coated resonator surface was used as reference to measure the background spectra.
3
Infrared Microscopy Measurements
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Measurements were recorded using a Hyperion 3000 IR microscope
(Bruker,
Fällanden, Switzerland) equipped with an ATR objective with
a circular contact area of 100 μm diameter.
(Bruker,
Fällanden, Switzerland) equipped with an ATR objective with
a circular contact area of 100 μm diameter.
4
FTIR Microspectroscopy of Red Blood Cells
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Analysis of RBCs was performed using FTIR microspectroscopy in transmission mode with a Bruker Hyperion 3000 IR microscope with a FPA detector attached to the Vertex 80 v spectrometer. Since cells were placed on a CaF2 window, a location adjacent to the sample at a clear, clean spot on that window was used for background signal collection.
An IR objective lens with 15× magnification was used that provides a pixel size equal to 2.7 μm2 (with 128 by 128 pixels in each direction of the FPA detector). The number of co-added scans were tested in order to ensure sufficient signal-to-noise ratio. 1024 scans provided a balance between good quality spectra within a reasonable amount of time (32 mins).
A spectral range of 3845 to 900 cm−1 was set with a spectral resolution of 8 cm−1. The zero filling factor was set to 2 and a Blackman-Harris 3-Term apodization function with phase resolution of 32 and power phase correction mode was selected for converting measured interferograms to final spectra.
From a single experiment, 16,384 spectra were collected from an area of approximately 345 × 345 µm2.
An IR objective lens with 15× magnification was used that provides a pixel size equal to 2.7 μm2 (with 128 by 128 pixels in each direction of the FPA detector). The number of co-added scans were tested in order to ensure sufficient signal-to-noise ratio. 1024 scans provided a balance between good quality spectra within a reasonable amount of time (32 mins).
A spectral range of 3845 to 900 cm−1 was set with a spectral resolution of 8 cm−1. The zero filling factor was set to 2 and a Blackman-Harris 3-Term apodization function with phase resolution of 32 and power phase correction mode was selected for converting measured interferograms to final spectra.
From a single experiment, 16,384 spectra were collected from an area of approximately 345 × 345 µm2.
5
Infrared Spectral Imaging of Hydrogels
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Infrared spectral imaging was carried out with a Hyperion 3,000 IR microscope coupled to a Tensor II FTIR spectrometer (Bruker Optik GmbH, Ettlingen, Germany). The microscope is equipped with an ATR objective (provided with a Germanium crystal; nD = 4.0) as well as with a 64 × 64 pixel focal plane array (FPA) detector. Spectral images of the hydrogel samples were recorded in the ATR mode. Each image covers a size of 32 × 32 μm. Taking into account the data of the ATR objective and the refractive index of PEGDA (nD = 1.47; the index of gelatin is roughly the same: nD = 1.5), the penetration depth of the probe light into the sample is about 760 nm at 1,093 cm−1, i.e., at the position of the most intense band in the spectrum of PEGDA corresponding to the asymmetric C-O-C stretching vibration. For an adequate signal-to-noise ratio, 128 accumulations were recorded for each image. The spectral resolution was set to 8 cm−1. For each hydrogel sample, several images were taken from various positions at both the top and the bottom side.
6
Characterization of Polymer Gradients via FTIR Microscopy
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A Bruker Hyperion 3000 IR microscope,
with light supplied from a Tensor 27 IR spectrometer (Bruker) and
equipped with a motorized and computer-controlled sample stage for
accurate positioning of the sample was used for collecting the infrared
reflection–absorption spectra. The objective used double surface
reflection with angles between 52 and 80° relative to the surface
normal. A nitrogen-cooled single-element mercury cadmium telluride
detector was used and the resolution was 4 cm–1.
Two-hundred interferograms were recorded at each measurement point
through a 100 × 200 μm2 aperture window with
the longer side perpendicular to the gradient direction when mapping
the samples by 250 μm intervals. Thirty spectra were taken under
N2 purging and all spectra were background corrected by
a concave rubberband method with 64 baseline points. This procedure
was used for the characterization of long P(MAA–DMAEMA) and
PDMAEMA gradients, as has also been described in more detail previously.21 (link),78 (link)
with light supplied from a Tensor 27 IR spectrometer (Bruker) and
equipped with a motorized and computer-controlled sample stage for
accurate positioning of the sample was used for collecting the infrared
reflection–absorption spectra. The objective used double surface
reflection with angles between 52 and 80° relative to the surface
normal. A nitrogen-cooled single-element mercury cadmium telluride
detector was used and the resolution was 4 cm–1.
Two-hundred interferograms were recorded at each measurement point
through a 100 × 200 μm2 aperture window with
the longer side perpendicular to the gradient direction when mapping
the samples by 250 μm intervals. Thirty spectra were taken under
N2 purging and all spectra were background corrected by
a concave rubberband method with 64 baseline points. This procedure
was used for the characterization of long P(MAA–DMAEMA) and
PDMAEMA gradients, as has also been described in more detail previously.21 (link),78 (link)
7
In-situ Activation and FTIR Analysis of MFM-126
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Single crystals of MFM-126 were loaded onto a ZnSe slide and placed into a Linkam FTIR600 variable temperature gas-tight cell fitted with ZnSe windows. The MOF sample was activated in situ under a flow of N2 whilst heating the Linkam stage to 413 K for 6 h. Partial pressures of zeolite-dried gases N2 and CO2 were controlled by varying the volumetric flow of the two gases via separate mass flow controllers. FTIR spectra were collected at the B22 MIRIAM beamline at Diamond Light Source using a polarized and highly bright synchrotron IR source connected to a Bruker Hyperion 3000 IR microscope with a 15× objective and MCT detector (liq. N2 cooled). Spectra (256 scans) were measured at room temperature with a 20 × 20 μm beam, in the spectral range of 4000–650 cm–1 (4 cm–1 resolution).
8
Infrared Spectroscopy Analysis of Rat Tendon Composition
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For tissue composition (n = 10 rats), the tendons that had been measured with SAXS were further embedded in paraffin and 2 independent 3µm-thick sections from the middle cross-section of each tendons were placed on BaF2 windows and evaluated with the D7 FTIR spectroscopy beamline at Max-IV laboratories, Lund, Sweden.
A Bruker 66 V FTIR spectrometer coupled to a Bruker Hyperion 3000 IR microscope was used with a focal plane array detector. Based on the light microscope image, a region (340 × 340 µm, divided into 64 × 64 elements) representing the centre of the tendon was chosen for analysis using 64 scans and a spectral resolution of 8 cm−1. The infrared spectra were collected at the range of 4000 to 900 cm−1. Collagen content was estimated from the peak area under the Amide I peak (Amide I peak; 1720–1585 cm−1). The ratio between mature and immature collagen cross-links were estimated from the 1660/1690 cm−1 intensity ratio58 (link). The proteoglycan content was estimated as the area under the peak located between 1125-970 cm−136 (link),37 (link) (see Fig.4a ). Please note that the content measures are not absolute measures but relative measures. The calculated area that is estimating molecular vibrations (see Fig. 4a Example spectrum).
A Bruker 66 V FTIR spectrometer coupled to a Bruker Hyperion 3000 IR microscope was used with a focal plane array detector. Based on the light microscope image, a region (340 × 340 µm, divided into 64 × 64 elements) representing the centre of the tendon was chosen for analysis using 64 scans and a spectral resolution of 8 cm−1. The infrared spectra were collected at the range of 4000 to 900 cm−1. Collagen content was estimated from the peak area under the Amide I peak (Amide I peak; 1720–1585 cm−1). The ratio between mature and immature collagen cross-links were estimated from the 1660/1690 cm−1 intensity ratio58 (link). The proteoglycan content was estimated as the area under the peak located between 1125-970 cm−136 (link),37 (link) (see Fig.
9
IR Characterization of CuNPs-Fe Complexes
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FT-IR and SEIRA spectra were recorded for a dried samples of CuNPs-Fe without and with Thr. The FT-IR spectrum were carried out for a dried solution of a 10−1-M Thr droplet on the calcium fluoride optical window. FT-IR and SEIRA spectra were recorded employing a Vacuum FT-IR VERTEX 70 V spectrometer (Bruker, Ettlingen, Germany) combined with the HYPERION 3000 IR microscope (Bruker Optics, Germany). The microscope was equipped with a liquid-nitrogen-cooled MCT (Mercury–Cadmium–Telluride) detector and a 15× magnification objective. The spectra were measured in reflectance mode covering the spectral range from 4000 cm−1 to 800 cm−1 (256 number of scans and 4 cm−1, spectral resolution). The spectra from the SEIRA were almost identical, except for small changes in the inten sities of some of the bands. In order to confirm the reproducibility of the observed phenomenon, the SEIRA spectra were recorded from three different areas.
10
FTIR Analysis of Cellular Biomolecules
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FTIR microspectroscopy analyses were performed on FACS-sorted O4+ OLCs aged 130 DIV and spheroids containing dopaminergic neurons aged 75 DIV. Cell pellets were washed and spread (1 μL) on the 1-mm-thick CaF2 spectrophotometric window and dried under nitrogen flow. For reproducibility, infrared (IR) spectra were taken from different areas of the cell pellet deposited on CaF2. The background spectra were measured from a clean area of the same CaF2 window, close to the cell pellet. Spectra were recorded on a Hyperion 3000 IR microscope (Bruker Scientific Instruments, Billerica, MA) coupled to a Tensor 27, which was used as the IR light source with 15Å∼ IR objective and mercury cadmium telluride detector. The measuring range was 900 to 4,000 cm−1, and the spectra collection was done in transmission mode at 4 cm−1 resolution from 250 to 500 coadded scans. All measurements were made at room temperature. For analysis of FTIR spectra, OPUS software (Bruker) and Orange (University of Ljubljana) were used after atmospheric compensation. Derivation of the spectra to the second-order using Savitzky-Golay of third polynomial order 3 with 9 smoothing points was used to unmask the peak corresponding to β-sheet structures (1,628 cm−1) and to eliminate the baseline contribution (77 (link)). To analyze β-sheet structural content, the 1,628 cm−1/1,656 cm−1 band ratio was studied (78 (link)).
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