The surface topography of the thin layer of polymer on the cover slides was characterized by atomic force microscopy (AFM) using a MultiMode 8-HR AFM (Bruker, Santa Barbara, CA) in air at room temperature. AFM was operated in tapping mode using Scanasyst-Air cantilevers (Bruker) with a nominal spring constant of 0.4 N.m-1 and a resonance frequency of 70 kHz. For each sample, AFM images of at least 5 individual areas (500 nm × 500 nm) were acquired. The collected images were analyzed by a custom-written MATLAB script to determine the interdomain distance and the size of the domains. A built-in MATLAB function “im2bw” was used to convert the AFM images into binary maps with a threshold at 20% above the average intensity of the image. Thereafter binary images were segmented with the built-in MATLAB function “bwonncomp” to identify the connected pixels that form domains. Finally, the built-in MATLAB function “regionprops” was used to determine the centre and the area of each domain.
Multimode 8 hr afm
Manufactured by Bruker
Sourced in Germany
The MultiMode 8-HR AFM is a high-resolution atomic force microscope designed for advanced nanoscale imaging and analysis. It offers precise and stable imaging capabilities for a wide range of sample types and applications.
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4 protocols using multimode 8 hr afm
1
Quantifying Polymer Surface Topography by AFM
2
Nanohybrid Imaging via Atomic Force Microscopy
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The samples were dried onto Muscovite mica sheets
for AFM analysis. To image the nanohybrids and the ThrC7 nanoassemblies,
AFM was conducted in the ScanAsyst mode on a Bruker Multimode 8HR
AFM. The tip used was a Bruker model RTESPA-525 made of 0.01–0025
Ω cm antimony (n) doped Si with a resonant frequency of 525
kHz and a spring constant of 200 N/m.
for AFM analysis. To image the nanohybrids and the ThrC7 nanoassemblies,
AFM was conducted in the ScanAsyst mode on a Bruker Multimode 8HR
AFM. The tip used was a Bruker model RTESPA-525 made of 0.01–0025
Ω cm antimony (n) doped Si with a resonant frequency of 525
kHz and a spring constant of 200 N/m.
3
GSS Protein-Small Molecule Crystal Analysis
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GSS protein was dissolved in 100 μM Tris–HCl (pH 8.0) and 1% DMSO, diluted to 0.1 μM, with 0.3 μM of saikosaponin A, saikosaponin D, saikogenin F, and saikogenin G solution, respectively. The protein solution was mixed with the small molecule ligand solution at 1:1 and 30 min was incubated at 37 °C. Then, the protein solution and the incubation solution were crystallized for 30 min at 37 °C on silicon wafers. After balance, MultiMode 8-HR AFM (Bruker, Berlin, Germany) was used to scan protein crystals and protein-small molecule complex crystals with parameters of 0.98 Hz, 20 μm × 20 μm in tap mode. The morphology, distribution, and aggregation of protein crystals on each silicon wafer were observed. NanoScope Analysis 1.8 was used to process the captured images.
4
Characterization of AgNW Thin Films
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Sheet resistance was measured using the 4-point probe system from Ossila. Optimization of the best photonic curing conditions to weld the AgNW film was done by only measuring the samples before and after in the same center spots, previously marked for uniformity of the measures. Rapid proof of crystallization of the TiO2 precursor was done following a modified version of rinse-in developing procedure reported elsewhere.2,31 (link) Plasma ageing was done using the same PE-100 PlasmaEtch system, set to 50 Watts for 40 seconds. Raman characterization is done using a WITec Alpha300 confocal Raman microscope equipped with a 60 mW fiber-coupled CW laser at 532 nm emission wavelength and a mechanical attenuator. SEM and EDS imaging was done using a SU8230 from Itachi. XRD was done using a Bruker D8 Advance, equipped with a Cu source. Atomic force microscopy analysis was done using a Bruker MultiMode8-HR AFM. Optical transmittance and haze analysis were done using a UV-VIS-NIR spectrophotometer PerkinElmer, Lambda 750 with an integrating sphere. Haze measures were performed following the procedure described in the ESI.†
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