20 μl of the fibril samples were diluted 1:300 and deposited on a freshly cleaved mica disc (Agar Scientific F7013). After 10 min incubation at room temperature, excess sample was removed by washing with 1 ml of 0.2 µm syringe filtered mQH20 and then dried under a gentle stream of N2. Samples were imaged using a Bruker Multimode AFM with a Nanoscope V controller and a ScanAsyst probe (Silicone nitride tip with tip height = 2.5–8 μm, nominal tip radius = 2 nm, nominal spring constant 0.4 N/m and nominal resonant frequency 70 kHz). Images were captured at a resolution of 4.88 nm per pixel scanned. All images were processed using the Nanoscope analysis software (version 1.5, Bruker). The image baseline was flattened using third order baseline correction to remove tilt and bow, and the data was saved as processed image files and raw data files, for recognition by the fibril tracing software. A larger number of images were collected for low sonication time point samples, as long fibrils are harder to measure due to a tendency to tangle and associate in larger structures (see Figure 2b ) that dissociate over extended periods of sonication. Processed image files were opened and analyzed using automated fibril tracing scripts written in Matlab (Xue, 2013 ).
Scanasyst probe
Manufactured by Bruker
The ScanAsyst probe is a specialized tip for use in Atomic Force Microscopy (AFM) systems. Its core function is to provide high-resolution surface imaging capabilities by utilizing advanced tip-sample interaction detection technology. The ScanAsyst probe is designed to maintain consistent performance and enable efficient, reliable data collection.
Automatically generated - may contain errors
Lab products found in correlation
Multimode afm, by Bruker (3 mentions)
F7013, by Agar Scientific (3 mentions)
Nanoscope 5 controller, by Bruker (3 mentions)
Nanoscope analysis software, by Bruker (3 mentions)
Nova nanosem 450, by Thermo Fisher Scientific (1 mentions)
Uv visible spectrometer, by PerkinElmer (1 mentions)
Tecnai g2, by Thermo Fisher Scientific (1 mentions)
Peak force tuna module, by Bruker (1 mentions)
5 protocols using scanasyst probe
1
Atomic Force Microscopy of Amyloid Fibrils
2
Structural and Electrochemical Analysis of Ag NWs and Ni(OH)2 NSs
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Structural analysis of the as-synthesized Ag NWs and Ni(OH)2 NSs was performed using an X-ray diffractometer with Cu Kα radiation (λ = 0.1541 nm). The microstructures were observed by transmission electron microscopy (TEM, FEI Tecnai G2) and scanning electron microscopy (SEM, FEI Nova NanoSEM 450). The sheet thickness of Ni(OH)2 was measured by atomic force microscopy (AFM, Bruker) using a Scanasyst probe. The chemical bonding states were determined by X-ray photoelectron spectroscopy (XPS, ESCALAB250Xi spectrometer). The transmittance of the TEs was determined using a PerkinElmer UV-visible spectrometer. The Rs values were determined using a Four-point Probe Resistance Tester (Zhuhai Kaivo Optoelectronic Technology Co., Ltd.). The electrochemical performance was investigated using the electrochemical workstation (Autolab PGSTAT302 N).
3
Morphological and Electrical Characterization of Mn/PPy Catalyst
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The morphology of Mn/PPy catalyst electrodeposited onto graphite discs was investigated by Field-Emission Scanning Electron Microscopy (FE-SEM) using an NVISION 40 Zeiss, equipped with a high resolution Gemini Field-Emission Gun and with an Oxford INCA 350 Xact Energy Dispersive X-Ray (EDX) Spectrometer. Details about the morphological features at the nanoscale and quantitative analysis of roughness and surface area were obtained with a Nanoscope III Multimode Atomic Force Microscope (AFM) (Bruker) in air using the ScanAsyst mode and the ScanAsyst probe (Bruker). On each sample 5 different square areas of sizes 1, 5, and 20 μm were scanned at rates of 0.7 and 1.5 Hz. The electrical conductivity of the sample was mapped by the PeakForce TUNA Module (Bruker) using a Pt/Ir probe (PF-TUNA 0.4 N/m, Bruker). AFM image analysis was carried out with the Nanoscope Analysis 1.5 program (Bruker).
4
Visualization of Amyloid Fibril Samples
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The fibril samples were diluted 1:100 for Sup35NM, and 20-μL droplets were deposited on freshly cleaved mica discs (Agar Scientific F7013). After 10-min incubation at room temperature, excess sample was removed by washing with 1 mL of 0.2-µm syringe-filtered mQ H2O, and the specimens were then dried under a gentle stream of N2(g). For Aβ42 fibrils, samples were diluted 1:10, and 10 μL were deposited on mica disk, let dry at room temperature, washed with 500 μL of mQ H2O, and then dried under a gentle stream of N2(g). Samples were imaged using a Bruker Multimode AFM with a Nanoscope V controller and a ScanAsyst probe (Silicone nitride tip with nominal tip radius = 2 nm, nominal spring constant 0.4 N/m, and nominal resonant frequency 70 kHz). Images were captured at a resolution of 4.88 nm per pixel scanned. All images were processed using the Nanoscope analysis software (version 1.5, Bruker). The image baseline was flattened using third order baseline correction to remove tilt and bow. Processed image files were opened and analyzed using automated scripts written in Matlab (60 ).
5
Atomic Force Microscopy of Amyloid Fibrils
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The fibril samples were diluted 1:100 for Sup35NM and 20 µl droplets were deposited on freshly cleaved mica discs (Agar Scientific F7013). After 10 min incubation at room temperature, excess sample was removed by washing with 1 ml of 0.2 µm syringe-filtered mQ H 2 O and the specimens were then dried under a gentle stream of N 2 (g). For Aβ42 fibrils, samples were diluted 1:10 and 10 µl were deposited on mica disc, let dry at room temperature, washed with 500 µl of mQ H 2 O and then dried under a gentle stream of N 2 (g). Samples were imaged using a Bruker Multimode AFM with a Nanoscope V controller and a ScanAsyst probe (Silicone nitride tip with nominal tip radius = 2 nm, nominal spring constant 0.4 N/m and nominal resonant frequency 70 kHz). Images were captured at a resolution of 4.88 nm per pixel scanned. All images were processed using the Nanoscope analysis software (version 1.5, Bruker). The image baseline was flattened using 3 rd order baseline correction to remove tilt and bow. Processed image files were opened and analyzed using automated scripts written in Matlab (Xue, 2013) . the data, and managed the research. The manuscript was written through contributions of all authors. * Median values in [psi -][PIN + ] yeast cells; † (Lund and Cox, 1981) ; ‡ (Lancaster et al., 2010)
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