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Su8100 scanning electron microscope

Manufactured by Hitachi
Sourced in Japan

The SU8100 is a scanning electron microscope (SEM) manufactured by Hitachi. It is designed to provide high-resolution imaging of a wide range of samples. The SU8100 utilizes an advanced electron optical system to generate a focused electron beam that scans the surface of the specimen, generating signals that are used to create a detailed image of the sample's topography and composition.

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18 protocols using su8100 scanning electron microscope

1

Scanning Electron Microscopy of FCP Powder

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The SEM of FCP was analyzed using a SU8100 scanning electron microscope (Hitachi, Tokyo, Japan). Briefly, the FCP powder sample was placed on a carbon-coated electrical film and coated with a sputtering of gold powder using a MC1000 sputter coater (Hitachi, Tokyo, Japan). Then, the FCP sample was imaged using magnifications of 500 and 5000 at an accelerating potential of 2 kV.
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2

Casein Microstructure Observation by SEM

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Following the method of Zhang A.Q. et al. [34 ], the microstructure of casein was observed with an SU8100 scanning electron microscope (Hitachi, Ltd., Tokyo, Japan). The freeze-dried casein powder was placed in a 1.5 mL centrifuge tube and fixed with glutaraldehyde for more than 4 h. Samples were washed 3 times at 10 min per time with a 0.1 mol/L phosphate buffer and were then fixed with 1% osmium tetroxide for 1 h.
The samples were gradient dehydrated with 50%, 70%, 80%, 90% and 100% ethanol for 10 min each time. The centrifugal tube was dried in a dryer for 12 h. Subsequently, the sample was taken out and adhered to a copper plate for conductive treatment. The sample was then observed by scanning electron microscope and the acceleration voltage was found to be 3 kV.
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3

Electrochemical Characterization of Modified Electrodes

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Scanning electron microscopy (SEM) measurements were performed on an SU8100 scanning electron microscope (Hitachi, Japan) with an accelerating voltage of 10 kV. X-photoelectron spectroscopy (XPS) data were obtained from a PHI5300 electron spectrometer (PE Ltd., Waltham, MA, USA) at 250 W, 14 kV and Mg Kα radiation. All electrochemical tests, including cyclic voltammetry (CV) and differential pulse voltammetry (DPV), were carried out on a PGSTAT302N Autolab electrochemical workstation (Metrohm, Herisau, Switzerland). The test adopted a conventional three-electrode system, including bare or modified GCE as the working electrode (the electrode’s size was 0.5 cm × 0.5 cm), a platinum sheet as the counter-electrode and an Ag/AgCl (saturated with KCl solution) electrode as the reference electrode. DPV test parameters were as follows: the step potential was 5 mV, the pulse amplitude was 25 mV, the pulse time was 0.05 s and the time interval was 0.2 s.
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4

Characterization of Modified Magnetic Nanoparticles and Pitch-based Adsorbents

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The methodology and equipment used for characterization, such as Fourier trans-form infrared spectroscopy (FT-IR, Platinum Elmer, USA), thermogravimetric analysis (TGA, STA449F3 Thermogravimetric instrument, NETZSCH, Germany), X-ray diffrac-tion patterns (XRD, Brock D8 ADVANCE, Brock, Switzerland), a scanning electron mi-croscope (SEM, Su8100 scanning electron microscope, Hitachi, Japan), a high-resolution transmission electron microscope (HRTEM, JEM-2100 F high-resolution transmission electron microscope, JEOL, Japan), Brunauer-Emmett-Teller analysis (BET, ASAP 2020 surface area and porosity analyzer, Micromeritics, USA), X-ray photoelectron spec-trometry (XPS, K-alpha device, Thermo Field), and Bruker 400M NMR carbon spectrum (13C NMR, Brock, Germany) analysis, were consistent with our previous work [30 (link)]. The structural analysis of modified magnetic nanoparticles (FT-IR, TGA, XRD, and SEM) and pitch-based adsorbents (FT-IR, TGA, XRD, SEM, TEM, VSM, and BET) were presented in detail [30 (link)].
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5

Scanning Electron Microscopy of Freeze-Dried Samples

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Micrographs were captured using an SU8100 scanning electron microscope (Hitachi, Tokyo, Japan). The freeze-dried samples were evenly distributed on the sample stage with a double adhesive tape and plated with a conductive gold layer (approximately 10 nm thick). The micrographs were obtained under low vacuum at an accelerating potential of 15 kV and were used to observe any damage to the sample surface.
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6

Characterization of 5-(4-aminophenyl)-10,15,20-triphenylporphyrin

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UV-Vis spectra were collected on a Cary 300 spectrometer. IR spectra were recorded on a Nicolet iS50 spectrometer using KBr pellets in the region of 4000–500 cm−1. 1H NMR spectra were recorded on a Varian Unity 400 (400 MHz) NMR spectrometer. Chemical shifts were reported on the d-scale relative to tetramethylsilane (TMS). Mass spectra were obtained using a Brucker Autoflex speed TOF/TOF Matrix-Assisted Laser Desorption Ionization Time of Flight Mass Spectrometry. Thermal analysis was recorded on Perkin-Elmer TG-7 apparatus (sample: 3–4 mg, heating rate: 10 °C/min, and nitrogen atmosphere). Fluorescence spectra were recorded with a HITACHI F-7000 spectrofluorometer. SEM figures were collected by the HITACHI SU8100 scanning electron microscope. A single-spindle electrostatic spinning machine was used to prepare electrospun fibers.
The reagents and solvents used in the experiment were of the commercial analytical pure grade and were used without further purification. The 5-(4-aminophenyl)-10,15,20-triphenylporphyrin was synthesized in the laboratory according to [21 (link)].
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7

Cell-Scaffold Characterization Workflow

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The
cells were seeded on each scaffold at a density of 1 × 105/cm2 and cultured for seven days. The cell–scaffold
complexes were then fixed with 2.5% glutaraldehyde, dehydrated by
gradually increasing grade of alcohol. They were then coated by gold
and observed by a SU8100 scanning electron microscope (Hitachi, Japan).
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8

Chitosanase-Mediated Ultrastructural Analysis

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The purified chitosanase SH21 was mixed with F. solani culture and incubated at 28 °C for 1 day with shaking at 180 rpm. Transmission and scanning electron microscopy (TEM and SEM) samples were prepared as described by Kang [41 ]. The morphological alterations and ultrastructure of the samples were observed using a SU8100 scanning electron microscope (HITACHI, Tokyo, Japan) and HT7800 transmission electron microscope (HITACHI, Tokyo, Japan), respectively.
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9

Visualizing Zinc-Dependent Bacterial Morphology

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WT and ΔadcAΔlmb strains were grown in CDM with 0.01 mM ZnSO4 overnight, washed three times in zinc-restricted CDM, and inoculated at OD600 = 0.2 in 15 mL Zn-deprived (without Zn) or Zn-containing CDM (with 0.01 mM Zn) for 5.5 h. The bacteria were harvested by centrifugation and cells were washed three times with PBS containing 0.25 mM EDTA. Next, bacteria were fixed with 2.5% glutaraldehyde at 4°C overnight. The samples were then treated with 1% osmium tetroxide for 2 h at room temperature and dehydrated in a serial dilution of ethanol. The dehydrated cells were coated with a 10-nm-thick gold layer for 30 s and observed by a SU8100 scanning electron microscope (Hitachi, Japan).
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10

Ultrastructural and Biochemical Analyses of Camellia migao Seeds

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The seeds from the four stages were fixed with 2.5 % glutaraldehyde in phosphate buffer (0.1 M, pH 7.4), dehydrated using a concentration series of ethanol (30 %, 50 %, 70 %, 80 %, 85 %, 90 %, 95 %, 100 %, and 100 % v/v) for 15 min, and then incubated with isoamyl acetate. The samples were treated with vacuum after air drying and were coated with gold in a vacuum evaporator (Quorum). The specimens were viewed and photographed under a HITACHI SU8100 scanning electron microscope. Seeds from the four stages described above were sampled to quantify the physiological parameters; three biological replicates were performed for the four stages. In brief, the soluble sugar content (SSC) and starch in seeds were determined using the anthrone method [57 (link)]. Soluble protein content was determined using the Coomassie brilliant blue G250 staining method [58 (link)]. A auto fat analyzer was used for C. migao lipid determination. MDA content was estimated using the thiobarbituric acid method, as reported by Hodges et al. [59 (link)], with minor modifications. SOD activity was analyzed using the nitroblue tetrazolium chloride method described by Lacan and Baccou [60 ], with minor modifications. POD activity was determined following the guaiacol method [61 ], with minor modifications. Catalase activity was determined using UV spectrophotometry [62 (link)], with minor modifications.
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