For SEM, exponentially growing cultures of Pdd RM-71 in TSB-1 and TSB-3 (OD600 of 0.55) were pelleted down by centrifugation (4,000 × g, 5 minutes, 4°C). Cells were fixed as previously described (27 (link)), sputter-coated with iridium, and imaged using an Ultra Plus ZEISS scanning electron microscope. For polysaccharide capsule visualization, sample processing and TEM analyses were conducted as previously described (28 (link)). Images were digitally recorded using a CCD digital camera Orius 1100 W (Gatan). Cell length, cell width, and capsule thickness at both salinities were determined by measuring 30 cells with the Fiji software (ImageJ version 1.51n) (43 (link)). Capsule thickness for each cell was calculated as the average of six measurements at different points. An unpaired t-test was used to determine statistical significance.
Ultra plus scanning electron microscope
Manufactured by Zeiss
Sourced in Germany
The Zeiss Ultra Plus scanning electron microscope is a high-performance imaging system that utilizes a focused electron beam to produce detailed images of small-scale structures and features. The core function of the Ultra Plus is to generate high-resolution, magnified images of samples, enabling users to analyze the surface topography and composition at the micro- and nanoscale level.
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Lab products found in correlation
Em ace600 coater, by Leica (1 mentions)
Isr 2600 plus integrating sphere, by Shimadzu (1 mentions)
Miniflex 600, by Rigaku (1 mentions)
Spectrum one spectrometer, by PerkinElmer (1 mentions)
Lambda 750, by PerkinElmer (1 mentions)
4155c semiconductor parameter analyzer, by Agilent Technologies (1 mentions)
Mfp 3d bio, by Oxford Instruments (1 mentions)
Oca 20 goniometer, by Dataphysics (1 mentions)
X 650 scanning electron microscope, by Hitachi (1 mentions)
Em ace600 sputter coater, by Leica (1 mentions)
15 protocols using ultra plus scanning electron microscope
1
SEM and TEM Analysis of Pdd RM-71 Cells
2
Pdd RM-71 Growth Characterization
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Exponentially growing cultures of Pdd RM-71 in TSB-1 at each temperature were stopped when they reached an OD600 of 0.55, cells were carefully pelleted down by centrifugation (4,000 g) and fixed for 3 h at 4°C in 4% paraformaldehyde and 2% glutaraldehyde in 0.1 M phosphate buffer, pH 7.4, and postfixed for 1.5 h in 1% osmium tetroxide in the same buffer. Samples were washed three times in dH2O, dehydrated using a series of graded ethyl alcohols, chemically dried using HMDS (hexamethyldisilazane) (Sigma), sputter-coated with iridium, and viewed and photographed in an Ultra Plus ZEISS scanning electron microscope.
3
Structural Analysis of Prepreg Tape
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Structural analysis of prepreg tape were carried out using a Zeiss® Optical Microscope (OM) and Zeiss® UltraPlus™ Scanning Electron Microscope (SEM). The SEM was run at a voltage of 10 kV and the secondary electron detector was used to image the sample, which was painted on the side with C paste to make it conductive for SEM characterization. SEM analysis provided information on the diameter, shape and aspect ratios of the fibres which subsequently helped in the determination of orientation across the regions of varying hardness within the material using Eqs. (2 ) and (3 ):
4
Hydrogel Formulation for Combination Therapy
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Gelation behavior in the presence of drugs was tested by vial inverting assay, where no flow in the presence of gravitation implies formation of gel. For DTX, the required amount of gelator and DTX (from ethanol stock) was taken in a vial. The solvent was removed under nitrogen and dried under vacuum. The mixture was dissolved in water with heating and sonication and allowed to cool for gelation. CPT entrapment was studied simply by mixing the water-soluble CPT formulation with hydrogelator in water. Drug concentration below which A13 gelator retains its ability to form gel is considered as the maximum drug loading efficiency. Hydrogel loaded with combination of DTX and CPT was prepared by mixing DTX with A13 gelator followed by addition of aqueous solution of CPT. Resultant suspension was heated until the solution turned clear and was allowed to cool at room temperature. The drug-loaded heated solution was taken in a syringe, allowed to cool to form the gel, and was used for animal models using 22- to 26-gauze needle. Gels were characterized for rheology using a Rheoplus MCR102 (Anton-Paar, Graz, Austria) rheometer and for morphology using an ultra plus scanning electron microscope (Carl Zeiss, Germany) as per the published protocols (24 (link)).
5
FESEM Imaging of Self-Assembled Peptides
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FESEM imaging was performed using a Zeiss ULTRA Plus
scanning electron
microscope operating at 3 kV. To avoid the morphology of the self-assembled
peptides from being obscured by the salts from the buffer, we used
Milli-Q water for scanning electron microscopy (SEM) imaging. Calculated
amounts of peptides were dissolved in the desired solvent (water or
TFE) and allowed to stand for at least 12 h at room temperature (ca.
25 °C). An aliquot of 2 μL of the peptide solution was
then drop-casted on a clean silicon wafer. Samples were allowed to
dry at room temperature in vacuum desiccators for at least 12 h, and
the dried film was sputter-coated with gold prior to imaging.
scanning electron
microscope operating at 3 kV. To avoid the morphology of the self-assembled
peptides from being obscured by the salts from the buffer, we used
Milli-Q water for scanning electron microscopy (SEM) imaging. Calculated
amounts of peptides were dissolved in the desired solvent (water or
TFE) and allowed to stand for at least 12 h at room temperature (ca.
25 °C). An aliquot of 2 μL of the peptide solution was
then drop-casted on a clean silicon wafer. Samples were allowed to
dry at room temperature in vacuum desiccators for at least 12 h, and
the dried film was sputter-coated with gold prior to imaging.
6
Characterization of Self-Assembled Nanoparticles
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Microscopy experiments
were performed to characterize the size of the self-assembled nanoparticles.
Samples were prepared carefully to minimize the effect of aggregation.
Then, 3–4 μL of peptide solutions was drop-casted on
different substrates followed by drying under high vacuum [Formvar
coated Cu grid for HRTEM, silicon wafer substrate for AFM, and field
emission SEM (FESEM)]. FESEM images were recorded using Zeiss Ultra
Plus scanning electron microscope after gold coating. AFM images were
recorded using Agilent instruments. The imaging was carried out in
tapping mode using a TAP-190AL-G50 probe from Budget sensors which
had a nominal spring constant of 48 N/m and the resonance frequency
of 190. HRTEM images were captured through a 1024 × 1024 digital
CCD camera using a Tecnai-G220-TWIN microscope instrument.
SEM samples were prepared by drop-casting NP and control peptide
solutions (3 μL, concentration: 1 mg/mL in 50:50 EtOH/H2O after lyophilization in 1 mL HFIP) on silicon wafers. Silicon
wafers were then dried at rt for 2 days and imaged. Similarly, HRTEM
samples were prepared by depositing NP solutions (3 μL, concentration:
1 mg/mL in 50:50 EtOH/H2O) on a copper grid, dried at rt
for 1 day, and then imaged. For AFM, samples were drop-casted on freshly
cleaved silicon wafers, air-dried at rt for 2–3 days. Tapping
mode was applied for AFM imaging according to the reported procedures.
were performed to characterize the size of the self-assembled nanoparticles.
Samples were prepared carefully to minimize the effect of aggregation.
Then, 3–4 μL of peptide solutions was drop-casted on
different substrates followed by drying under high vacuum [Formvar
coated Cu grid for HRTEM, silicon wafer substrate for AFM, and field
emission SEM (FESEM)]. FESEM images were recorded using Zeiss Ultra
Plus scanning electron microscope after gold coating. AFM images were
recorded using Agilent instruments. The imaging was carried out in
tapping mode using a TAP-190AL-G50 probe from Budget sensors which
had a nominal spring constant of 48 N/m and the resonance frequency
of 190. HRTEM images were captured through a 1024 × 1024 digital
CCD camera using a Tecnai-G220-TWIN microscope instrument.
SEM samples were prepared by drop-casting NP and control peptide
solutions (3 μL, concentration: 1 mg/mL in 50:50 EtOH/H2O after lyophilization in 1 mL HFIP) on silicon wafers. Silicon
wafers were then dried at rt for 2 days and imaged. Similarly, HRTEM
samples were prepared by depositing NP solutions (3 μL, concentration:
1 mg/mL in 50:50 EtOH/H2O) on a copper grid, dried at rt
for 1 day, and then imaged. For AFM, samples were drop-casted on freshly
cleaved silicon wafers, air-dried at rt for 2–3 days. Tapping
mode was applied for AFM imaging according to the reported procedures.
7
Nanofibrous Layer Morphology Analysis
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The morphology of the nanofibrous layers was studied using a Zeiss ULTRA PLUS scanning electron microscope (ZEISS, Oberkochen, Germany). The samples were coated with a very thin layer of Au and Pd in a Leica EM ACE600 coater (Leica, Wetzlar, Germany). Images were acquired using an SE detector; the working distance ranged from 4 mm to 6 mm, and the accelerating voltage was 3.5 kV. Randomly selected images representative of the entire implant area covered in a nanofibrous layer were used to measure the diameters of 80 individual nanofibers in the ImageJ software and the results were represented with a histogram and defined with mean +/- SD. The deposited nanofibrous layers were evaluated first immediately after the spinning process and again after their cross-linking and the subsequent lyophilization in order to determine how these processes affect the morphology of deposited nanofibers. Furthermore, the ability of the deposited material to retain its fibrous structure was assessed.
8
Structural and Optical Characterization of Photocatalysts
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Morphological studies were conducted by an Ultra Plus scanning electron microscope (SEM) (Zeiss, Germany). Structural characterization of BiVO4, GO and rGO was performed using X-ray diffraction (XRD) on a Miniflex 600 equipped with D/teX Ultra 2 silicon strip detector (Rigaku, Tokyo, Japan). Fourier transform infrared (FTIR) spectra were recorded on a Spectrum One spectrometer (Perkin Elmer, Waltham, MA, USA) in the range of 4000 cm−1 to 650 cm−1 using attenuated transmission reflectance technique. The diffuse reflectance measurements were taken on FTO-coated photoelectrodes using a UV-VIS spectrometer 2600i equipped with an ISR-2600Plus integrating sphere (Shimadzu, Kyoto, Japan).
9
Characterization of Aβ Fibril Morphology
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A scanning electron microscope (SEM; Ultra plus Scanning Electron Microscope from Carl Zeiss NTS) (Manufacturer, City, State abbr. if USA, Country), operating at 4 kV with secondary electrons, in high-vacuum mode, was used to observe the morphological properties of the Al–peptide complexes. The SEM studies were performed on samples dried on small glass slides, fixed on copper supports using carbon tape, and covered with a thin layer of platinum to avoid electrostatic charging. We used SEM to characterise the fibril morphology of aggregates formed by Aβ(1–16)A36,13,14 and Aβ(1–16)S36,13,14 upon incubation with aluminium sulphate (peptide concentration 256 μM; 1:1 molar ratio) for 24 h at 25 °C.
10
Comprehensive Material Characterization Techniques
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TEM and HRTEM measurements were carried out on JEM1011 operated at 80 kV and JEM-2100F operated at 200 kV, respectively. SEM was carried out on Ultra plus scanning electron microscope (Zeiss) with 10 kV acceleration voltage. UV-vis-NIR absorption spectra were measured on UV-vis-NIR spectrometer Lambda 750 (Perkin Elmer). XRD was carried out with a custom-built molybdenum Kα X-ray reflectometer/diffractometer. The samples were measured at a fixed incidence angle of 10°, and intensities at different scattering angles (2θ) were recorded from 10 to 60°in 2500 steps (0.02°/step) for 10 s each using a point detector (NaI scintillation counter). EA (C, H, N) test was measured with the Heraeus Elementar Vario EL instrument.
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