The largest database of trusted experimental protocols

32 protocols using s 4800 electron microscope

1

XRD and SEM Characterization of Reaction Precipitates

Check if the same lab product or an alternative is used in the 5 most similar protocols
After DCM extraction, the reaction precipitate was washed with deionized water and dried in a vacuum oven at 60 °C for further characterization. XRD patterns were obtained on an SHIMADZU XRD-6100 PC with Cu Kα radiation (λ = 1.54184 Å) in steps of 0.02° and an accumulation time of 0.6 s per step at 40 kV and 40 mA. The peak identifications were carried out based on the reference patterns reported in the Power Diffraction File published by the International Centre for Diffraction Data. Scanning electron microscopy photographs were taken on a Hitachi s-4800 electron microscope at an acceleration voltage of 5 kV.
+ Open protocol
+ Expand
2

Characterizing Multilayer Film Thickness

Check if the same lab product or an alternative is used in the 5 most similar protocols
During the preparation of multilayer films, the changes in thickness were followed using spectroscopic ellipsometry (M-2000 DITM, J.A. Woollam). This experiment was performed on silicon wafers. The continuing wavelength ranging from 124 nm to 1700 nm and selected the angle of incidence of both 65ºand 70º for ellipsometry measurements. We selected ∆ and Ψ values surveyed at a wavelength of 600–1700 nm for analysis. The thickness of multilayer films was determined using the Cauchy model. We set parameters An and Bn for the Cauchy layer at 1.45 and 0.01, respectively, as fit parameters. Then, the thickness that fit the multilayer films was fabricated such that it can be automatically calculated. Further, the morphology of the multilayer films was examined under Hitachi S-4800 electron microscope (Tokyo, Japan) at an acceleration voltage of 10kV. Finally, images were adjusted for clear visualization of the multilayer films and photographed.
+ Open protocol
+ Expand
3

Characterization of Porous Materials

Check if the same lab product or an alternative is used in the 5 most similar protocols
FTIR spectra were collected in ATR mode on a Spectrum II spectrometer (Perkin-Elmer). The powder XRD patterns were collected with a PANalytical X’Pert Pro MPD diffractometer (Cu Kα1 = 0.1540598 nm). The SEM images were obtained with a Hitachi S-4800 electron microscope. EDX was done on an Oxford Instruments X-MaxN SDD instrument. Nitrogen adsorption and desorption isotherms were measured at 77 K with a Micrometrics TriStar 3000 apparatus; the specific surface area was determined by the BET method in the 0.05–0.25 P/P0 range. The mesopore volume and pore size distribution were obtained by the Barrett–Joyner–Halenda (BJH) method from the desorption branch.
Solid-state 31P magic angle spinning (MAS) NMR experiments were performed on a Varian VNMRS 400 MHz (9.4 T) spectrometer using a 3.2 mm Varian T3 HXY MAS probe. Single pulse experiments were carried out with a spinning rate of 20 kHz, a 90° excitation pulse of 3 μs, a recycle delay of 30 s and 100 kHz spinal-64 1H decoupling. 200 transients were recorded. The 31P chemical shift was determined using an external reference, hydroxyapatite Ca10(PO4)6(OH)2, at 2.8 ppm (with respect to H3PO4, 85 wt % in water).
+ Open protocol
+ Expand
4

SEM Analysis of FeAg2@MOF

Check if the same lab product or an alternative is used in the 5 most similar protocols
SEM elemental analysis was
carried out for Fe3+Ag02@MOF using a HITACHI S-4800 electron microscope coupled with an EDX detector.
Data was analyzed with QUANTAX 400.
+ Open protocol
+ Expand
5

Optimizing Solvent Evaporation in Microparticle Synthesis

Check if the same lab product or an alternative is used in the 5 most similar protocols
To control the evaporation rate of solvent from MPs, multiple process conditions were tested including sonication time and total sample volume (50, 100, and 200 mL; 5 v/v% of polymer stock solution). Specifically, the sample temperature was measured after a continuous sonication (sonication cycle on throughout) at R.T. (i.e., no external temperature control) and in iced water for varying total sonication time durations (5, 10, 15, 30, and 60 min). Morphologies of MPs prepared by sonicating 100 mL of samples for 5, 30, and 60 min were analyzed by scanning electron microscope (SEM; S4800 Electron Microscope; Hitachi, Japan) to investigate the effect of sample temperature on the pore forming properties of MPs.
+ Open protocol
+ Expand
6

Morphological Characterization of Microparticles

Check if the same lab product or an alternative is used in the 5 most similar protocols
The morphology of the MPs was characterized using the scanning electron microscope (SEM; S4800 Electron Microscope; Hitachi, Japan). The pore-particle size ratio of the MPs (acquired from 300 measurements) was measured from the image analysis using Adobe Photoshop CS3. The image analysis was performed to study the effects of the fabrication protocol on the samples, the effects of solvent evaporation on the pore formation or pore extension in MPs, and to evaluate the pore closure efficiency of the freeze-drying process. The SEM images were also used for measuring the number ratio of the number of pored particles divided by the total number of particles to monitor the effect of the solvent evaporation process on the extension or formation of the surface pores on MPs. In a typical procedure, MPs in the powder form were placed uniformly on a double-sided carbon tape. The sample was coated with a 7-nm gold layer to minimize the charging effect and observed at 15 kV (20 µA). To observe the pH-dependent change in morphology of MPs, 40 µL of the sample solution obtained at each time interval. This solution was carefully dropped on a glass coverslip and the major portion of the water was quickly removed by a filter paper using the blotting technique, and the sample was further dried in a fume hood at RT.
+ Open protocol
+ Expand
7

Multimodal Characterization of Materials

Check if the same lab product or an alternative is used in the 5 most similar protocols
X-ray diffraction (XRD) measurements were recorded in the range of 10° to 80° (2θ) on a Rigaku Ultima IV diffractometer using Cu-Kα radiation (Tokyo, Japan). Scanning electron microscopy (SEM) images were obtained using a Hitachi S-4800 electron microscope (Tokyo, Japan). The elemental composition of the samples was measured by an energy-dispersive X-ray spectrometer (EDX) attached to a scanning electron microscope (Tokyo, Japan). The high-resolution transmission electron microscopy (HRTEM) images of the samples were taken on a JEOL JSM-3010 microscope (Tokyo, Japan). N2 adsorption/desorption isotherms were examined on a Quantachrome Quadrasorb SI apparatus at 77 K (Boynton Beach, FL, USA).
+ Open protocol
+ Expand
8

E. coli Morphological Changes by SibaCec

Check if the same lab product or an alternative is used in the 5 most similar protocols
Bacteria E. coli ATCC 25922 were incubated with SibaCec (1 × MIC) diluted in phosphate buffered saline (PBS) at 37 °C for 45 min. Bacteria incubated with PBS was used as negative control. After centrifugation, bacteria pellets were fixed with 2.5 % glutaraldehyde solution for 2 h at 4 °C and then postfixed in 1 % osmium tetroxide for 2 h. Dehydration was carried out with a graded series of alcohols. Bacteria were mounted onto aluminium stubs and sputtered with gold. Images were visualized in a Hitachi S-4800 electron microscope.
+ Open protocol
+ Expand
9

Preparation and Imaging of Transgenic Mouse Embryo Heads

Check if the same lab product or an alternative is used in the 5 most similar protocols
Preparation of E11.5 CRE-negative control, Tfap2HET and Tfap2NCKO littermate heads and imaging was performed as previously described (Van Otterloo et al., 2022 (link)). Briefly, samples were fixed in 4% paraformaldehyde (PFA) and then rinsed in 1×PBS. Subsequently, samples were rinsed in deionized H2O, air-dried for at least 3 days, mounted on a scanning electron microscopy (SEM) stub, and sputter coated for 4.5 min at 5 mA using a gold/palladium target in an Emitech K550X sputter coater. Scanning electron micrographs were acquired using a Hitachi S4800 electron microscope operated in high-vacuum mode at 1.8 kV. Imaging was performed through the University of Iowa Central Microscopy Research Facility workflow.
+ Open protocol
+ Expand
10

Ultrastructural Analysis of Particulated Cartilage

Check if the same lab product or an alternative is used in the 5 most similar protocols
Scanning (SEM) and transmission (TEM) electron microscopy techniques were employed for the ultrastructural analysis of particulated cartilage embedded in PRGF. Briefly, the samples collected at one-week intervals were rinsed with PBS, fixed with 2% glutaraldehyde in a 0.1 M cacodylate buffer for 4 h and washed 3 times in a cacodylate-sucrose buffer (0.1 M cacodylate, 6.5% sucrose, pH 7.4). Subsequently, the samples were post-fixed with osmium tetroxide (1% OsO4 in 0.1 M cacodylate) for 1 h at 4 °C in the dark and washed in 0.1 M cacodylate. Finally, the samples were dehydrated using increasing ethanol concentrations (30, 50, 70, 96, and 100%). At this point, the samples were separated for each of the two imaging techniques (SEM and TEM) and processed independently. For SEM, the samples were incubated twice in hexamethyldisilazane for 10 min and allowed to dry prior to examination with a Hitachi S-4800 electron microscope. For TEM imaging, the samples were incubated in propylene oxide for 1 h, then in increasing concentrations of Epon resin, and finally embedded in Epon. Ultrathin sections were stained with uranyl acetate and lead citrate and examined using a Philips EM208S electron microscope.
+ 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!