The largest database of trusted experimental protocols

21 protocols using cm10 microscope

1

Characterization of Functionalized SBA-15 Nanocomposites

Check if the same lab product or an alternative is used in the 5 most similar protocols
Chemical compounds were purchased from Sigma–Aldrich and Merck companies with a commercial grade and used as received without further purification. Melting points were determined in open capillaries using an electrothermal digital melting point apparatus and were uncorrected. Fourier transform infrared (FT-IR) spectra were recorded on a JASCO 4200-A spectrometer with KBr pellets. 1HNMR and 13CNMR spectra were recorded on a Bruker spectrometer (300–500 MHz) using DMSO-d6 as a solvent and Me4Si as an interior standard. The morphology of the functionalized SBA-15 was investigated using a Leica Cambridge S 360 scanning electron microscope (scanning electron microscopy (SEM) and field emission scanning electron microscopy (FE-SEM)). Transmission electron microscopy (TEM) images were recorded on a Philips CM10 microscope with an acceleration voltage of 100 kV. N2 adsorption–desorption isotherms of SBA-15 nanocomposites were measured at the temperature of liquid nitrogen using a Micromeritics system (made in the United States). The Brunauer–Emmett–Teller surface area of the nanoparticles was calculated using the BET method.
+ Open protocol
+ Expand
2

Characterization of Triblock Copolymer Nanostructures

Check if the same lab product or an alternative is used in the 5 most similar protocols
1H NMR spectra were recorded
using a Bruker AC-400 NMR at room temperature by dissolving the samples
in CDCl3. The Fourier transform infrared spectra (FTIR)
were obtained using Bruker Vertex 70. Surface tension was measured
via the tensiometer Data Physics DCAT 21 system at room temperature.
The dynamic light scattering (DLS) experiments was performed on a
Brookhaven BI-200SM goniometer system equipped with a 522-channel
BI9000AT digital multiple τ correlator. The inverse Laplace
transformation of REPES in the Gendist software package was used to
analyze the time correlation functions with a probability of reject
set at 0.5. The deionized water used was from a Millipore Alpha-Q
purification system equipped with a 0.22 μm filter. A 0.8 μm
filter was used to remove dust before light scattering experiments,
and the experimental temperature was controlled by a PolyScience water
bath. The transmission electron microscopy (TEM) was conducted on
a Philips CM10 microscope at an acceleration voltage of 60 keV. The
TEM samples were prepared by drop coating the supernatant of triblock
copolymer aqueous solution (0.01 wt %) prepared by solvent exchange
onto copper grids (200 mesh coated with copper) and then drying the
samples overnight at ambient temperature.
+ Open protocol
+ Expand
3

Ultrastructural Analysis of Synaptic Vesicles

Check if the same lab product or an alternative is used in the 5 most similar protocols
Neurons were fixed with 1.2% glutaraldehyde in 0.1 M sodium cacodylate buffer, postfixed in 1% OsO4, 1.5% K4Fe(CN)6, 0.1M sodium cacodylate, en bloc stained with 0.5% uranyl magnesium acetate, dehydrated, and embedded in Embed 812. Where indicated, HRP reactions were developed with diaminobenzidene and H2O2 after the glutaraldehyde fixation step. Electron microscopy reagents were purchased from Electron Microscopy Sciences. Ultrathin sections were observed in a Philips CM10 microscope at 80 kV and images were taken with a Morada 1kx1k CCD camera (Olympus). For quantification, 20–30 pictures from each sample were used for calculating the C2-XL-HRP-labeled synaptic vesicles. 200–500 vesicles were measured for synaptic vesicle diameter analysis.
+ Open protocol
+ Expand
4

Correlative Light and Electron Microscopy of Neuronal Synapses

Check if the same lab product or an alternative is used in the 5 most similar protocols
Plasmids encoding SNAP-CLC were electroporated into dissected neuronal suspensions using an Amaxa Nucleofector Kit (Lonza) at DIV0 before plating on 35-mm gridded, glass-bottom MatTek dishes (part no. P35G-1.5-14-CGRD). At DIV14, neurons were stained with 0.5 μM Janelia Fluor 549 at 37 °C for 1 h, followed by incubation in original culture medium at 37 °C for 2 h before fixation for immunofluorescence or CLEM. Labeled neurons were imaged and their coordinates on the MatTek dishes recorded using fluorescence microscopy and bright-field differential interference contrast microscopy, respectively. Then neurons were fixed with 2.5% glutaraldehyde in 0.1 M sodium cacodylate buffer, postfixed in 0.1 M sodium cacodylate buffer containing 1% OsO4 and 1.5% K4Fe(CN)6 (Sigma-Aldrich), en bloc stained with 2% aqueous uranyl acetate, dehydrated, and embedded in Embed 812. The nerve terminals expressing SNAP-CLC were relocated (based on the prerecorded coordinates), sectioned, and imaged. Ultrathin sections (60 to 80 nm) were observed with a Philips CM10 microscope at 80 kV, and images were obtained with the iTEM soft imaging system and a Morada 1k × 1k CCD camera (Olympus). Except when noted otherwise, all reagents for EM were obtained from EMS.
+ Open protocol
+ Expand
5

Negative Staining of Phage Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
For negative staining, 5 µL of PEG purified phage sample (~ 6 × 106 pfu/ml) was applied onto glow-discharged carbon coated grids and incubated for five minutes at room temperature. Grids were washed with 5 µL of deionized water before incubating for 2 min with a 1% uranyl acetate solution. Electron micrographs were taken using a Phillips CM-10 microscope at the Manawatu Microscopy and Imaging Centre (MMIC, Massey University, Palmerston North, New Zealand)55 (link).
+ Open protocol
+ Expand
6

Negative Staining for Structural Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Negative staining was performed following the described procedure (Harris and De Carlo, 2014). Carbon‐coated copper grids (Ted Pella, Inc. Formvar W/CARB on 200 M CU; Prod No. 01801) were used with 2.5% w/v ammonium molybdate, pH 5‐7. A Philips CM10 microscope running at 60.0 kV was used. TEM micrograph images were analyzed using imageJ (Schneider et al., 2012). To measure inter‐unit spacings, five separate square grids of 15 x 15 particles were identified and the average center‐to‐center distance was calculated for each axis.
+ Open protocol
+ Expand
7

Ultrastructural Analysis of Oral Pathogens

Check if the same lab product or an alternative is used in the 5 most similar protocols
The OKF6 WT, MOCK and T2R14 KD cells treated with S. aureus and S. mutans were fixed with 3% gluteraldehyde in 0.1 M Sorensen’s buffer for 3 h. After fixation the cells were suspended in sucrose solution and stored at 4 °C for processing. The above fixed cell suspensions were embedded into plastic resins and thin sections (90–100 nm) are placed on mesh copper grids. The copper grids are finally stained with osmium tetroxide and uranyl acetate. The grids were imaged by using a Philips CM10 microscope at a magnification of 10,500×.
+ Open protocol
+ Expand
8

Negative Staining of Axoneme Samples

Check if the same lab product or an alternative is used in the 5 most similar protocols
4 μL of the splayed axoneme sample was adsorbed to glow-discharged, carbon-coated copper grids (Electron Microscopy Sciences, CF200-Cu) for 1 min before blotting with filter paper, and washed twice with 4 μL of 1.5% uranyl formate. The grids were then incubated with a third application of 4 μL 1.5% uranyl formate for 1 min, blotted, and air-dried before storing. Negative-stain grids were imaged using a Gatan UltraScan 894 (2k × 2k) CCD camera on a Phillips CM10 microscope equipped with a Tungsten filament operated at 100 kV.
+ Open protocol
+ Expand
9

Characterization of Nanomaterials Using Advanced Techniques

Check if the same lab product or an alternative is used in the 5 most similar protocols
To characterize the nanomaterials, powder X‐ray diffraction (XRD), thermogravimetric analysis (TGA), elemental analysis (EA), transmission electron microscopy (TEM), N2 adsorption‐desorption, and UV‐visible spectroscopy techniques were used. The following equipment was used: X‐ray measurements were performed on a Bruker AXS D8 Advance diffractometer using Cu‐Kα radiation. Thermogravimetric analyses were carried out on a TGA/SDTA 851e Mettler Toledo equipment, using an oxidant atmosphere (Air, 80 ml/min) with a heating program consisting on a heating rate of 10°C/min from 393 K to 1,273 K and an isothermal heating step at this temperature for 30 min. TEM images were taken with a Philips CM10 microscope working at 100 kV. N2 adsorption–desorption isotherms were recorded on a Micromeritics ASAP2010 automated sorption analyzer. The samples were degassed at 120°C under vacuum overnight. The specific surface areas were calculated from the adsorption data in the low pressures range using the BET model. Pore size was determined by following the BJH method. UV‐visible spectroscopy was carried out with a Lambda 35 UV/vis spectrometer (Perkin‐Elmer Instruments), and fluorescence spectroscopy was performed with a JASCO spectrofluorometer FP‐8300.
+ Open protocol
+ Expand
10

Multimodal Characterization of Catalysts

Check if the same lab product or an alternative is used in the 5 most similar protocols
Fourier-transform infrared spectrum was carried out in the region 400–4000 cm−1 by a JASCO 6300D instrument. Thermogravimetric (TGA) analyses were regulated using a Perkin-Elmer -6000 instrument. The scanning electron microscope (SEM) images were taken using a Hitachi S–4800 fields. The transmission electron microscopy (TEM) images were recorded with a Philips CM10 microscope. The XRD measurement patterns were collected a Bruker D8-advance X-ray diffract meter with Cu Kα radiation. Raman spectroscopy was determined on a Renishaw Raman system model 1000 spectrometer with an excitation wavelength of 514 nm. The yields were estimated by gas chromatography tests that were by a Shimadzu (GC-16A) equipped with an FID detector. The metal content of the catalysts was recorded by utilizing inductively coupled plasma optical emission spectroscopy (ICP-OES) analysis conducted on a PerkinElmer emission spectrometer.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!