Nanosurgical manipulation was carried out by pushing the tip of an AFM cantilever onto the sample, then moving the tip sideways so as to dislocate targeted parts of the molecular complex of titin [43 (link)]. First, a control AFM image was collected, with a Cypher ES scanner (AsylumResearch, Santa Barbara, CA, USA), in tapping mode at a setpoint 60–70% of the cantilever’s free oscillation amplitude so as to prevent unwanted mechanical damage of the sample. Typical scanning rates were 0.4–1.2 Hz. Silicon-nitride cantilevers (OMCL-AC160TS-R3, Olympus, Tokyo, Japan) were employed with a tip radius of 7 nm and nominal spring constant of 27 N/m. Subsequently, the starting point, the direction, the distance and speed of the AFM tip movement were adjusted. The probe was pushed against the surface, in contact mode, with force ranging between 150–600 nN. The speed and distance of probe movement was varied between 10–1000 nm/s and 10–300 nm, respectively. Finally, a second AFM image was collected, with scanning parameters identical to those of the initial scan, to reveal the structural changes caused by the nanosurgical manipulation.
Omcl ac160ts r3
Manufactured by Olympus
Sourced in Japan, United States
The OMCL-AC160TS-R3 is an automated cell counter and analyzer system designed for cell counting and viability analysis. The device uses advanced imaging technology to capture and analyze cell samples, providing accurate and reliable cell count and viability data.
Automatically generated - may contain errors
Lab products found in correlation
Nanoscope iiia tapping mode afm, by Veeco (3 mentions)
Multimode 8, by Bruker (2 mentions)
Cary 50 spectrophotometer, by Agilent Technologies (1 mentions)
Ftir 600, by Linkam (1 mentions)
Nanowizard 3 atomic force microscope, by Bruker (1 mentions)
Agilent 5500, by Agilent Technologies (1 mentions)
Lobind reaction tube, by Eppendorf (1 mentions)
Cypher s afm, by Oxford Instruments (1 mentions)
Mfp 3d origin, by Oxford Instruments (1 mentions)
Cypher es afm, by Oxford Instruments (1 mentions)
16 protocols using omcl ac160ts r3
1
Nanosurgical Manipulation of Titin
2
QCM and AFM Analysis of DNA Hybridization
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The QCM chips were incubated separately with DNA samples including “PM”, “1 M” and “control” which were target DNA samples consisting of different DNA sequences and had different affinity to hybridize with probe DNA on the QCM chips. All AFM measurements were accomplished on an equipment (Multimode 8, Bruker, USA) in tapping mode and with a silicon cantilever (OMCL-AC160TS-R3, Olympus). The analyses of AFM data were accomplished by the Gwyddion software versions 2.54.
3
Temperature-Dependent Optical and Structural Characterization
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Temperature-dependent absorbance spectra of the films, deposited on fused silica substrates, were collected at wavelengths between 200 and 800 nm, using a Cary 50 spectrophotometer (Agilent Technologies) and a heating/cooling stage (Linkam Scientific Instruments, FTIR600). Spectra were acquired in the 20–120 °C range with a scan rate of 1 °C min−1. AFM topography measurements were performed using a Cypher-ES microscope (Oxford Instruments) in amplitude-modulation mode in ambient air, using OMCL-AC160TS-R3 (Olympus) probes. Scanning electron microscopy (SEM) images of the metallic wires were recorded using a JSM-7800F Prime microscope (JEOL) operated at 5 kV.
4
AFM Imaging of Amyloid Fibril Formation
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For AFM imaging, 2 μl samples were taken out of the wells at the end of the ThT aggregation assays, put onto a freshly cleaved muscovite mica surface and dried during incubation for 10 min under the clean bench. Subsequently, the samples were washed with 100 μl ddH2O in three steps and dried with a stream of N2 gas. Imaging was performed in intermittent contact mode (AC mode) in a JPK NanoWizard 3 atomic force microscope using a silicon cantilever with silicon tip (OMCL-AC160TS-R3, Olympus) with a typical tip radius of 9 ± 2 nm, a force constant of 26 N/m and resonance frequency around 300 kHz. The images were processed using JPK DP Data Processing Software (version spm-5.0.84).
5
AFM Characterization of Protein Nanostructures
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In AFM measurement, muscovite mica was freshly cleaved by tape and used as substrate. PFF, 8 times diluted at a volume of 10 μL, were deposited on freshly cleaved mica for 30 min. Then, the excess sample was removed, and the mica was rinsed once with Milli-Q water and later dried in ambient condition for 1 h before measurement. The AFM morphology measurements were completed using an equipment (Multimode 8, Bruker Co., Ltd., USA) in tapping mode with ultra-sharp silicon cantilevers (OMCL-AC160TS-R3; Olympus). During the measurements, the scan rate was set at 1 Hz. Resonant frequency was set at 300 kHz. The resolution of all AFM images was 512 × 512 pixels.
6
Atomic Force Microscopy of Protein Fibrils
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AFM images were taken with a Nanowizard 3 atomic force microscope (JPK, Berlin, Germany) in intermittent contact mode (AC mode) in air, using silicon cantilever and tip (OMCL-AC160TS-R3, Olympus, Hamburg, Germany) with a typical tip radius of 9 ± 2 nM, a force constant of 26 N/m and a resonance frequency of approximately 300 kHz. The images derive from a manual observer-blind estimation, and provide qualitative characteristics. The image processing was performed using JPK data processing software (version spm-5.0.84): for each of the presented height profiles, a polynomial fit was subtracted from each scan line first independently and then using limited data range. For the sample preparation, solutions containing fibrils were diluted to a concentration of 1 µM (in monomer equivalents) in water and 5 μL samples of the diluted solution were deposited on freshly cleaved muscovite mica and left to dry for at least 30 min. The samples were carefully washed with 50 µL of double distilled H2O and then dried again with a stream of N2 gas before imaging.
7
Nanoscale Surface Topography Analysis
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AFM was used to examine the surface topography and nanoroughness of the films transferred to solid substrates using an AFM from Asylum Research (Santa Barbara, CA, USA) equipped with a silicon cantilever (OLYMPUS OMCL AC160TS-R3). The scans were evaluated with ImageJ software.
8
Characterizing Metamaterial Nanostructures via AFM
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The metasurface topography was characterized using the fast-scanning atomic force microscope Cypher (Oxford Asylum Research), equipped with standard micro cantilever OMCL-AC160TS-R3 (Olympus, Oxford Instruments). The OMCL-AC series has a tetrahedral tip on the exact end of the cantilever. The nominal probe spring constant was equal to 26.1 N/m and the tip radius was 7 nm. Maps visualizing the metamaterial nanostructure were obtained by adopting a contact mode, and then they were processed graphically by employing the IGOR Pro ver. 6.32 A software prepared by the AFM manufacturer. Furthermore, to obtain a full range of colors in addition to highlighting the architecture of nano-elements, the 3D image level was slightly lowered, which is why we see negative values on the scale showing the height.
9
Atomic Force Microscopy of α-Synuclein
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The α-synuclein PFF solution was deposited on freshly cleaved mica (The Nilaco Corporation, Tokyo, Japan) and incubated for 10 min. After washing the mica with distilled water, sample imaging was performed under ambient conditions at room temperature using a NanoScope IIIa Tapping Mode AFM (Veeco, Plainview, NY, USA) and microcantilever OMCLAC160TS-R3 (Olympus, Tokyo, Japan).
10
Graphite Exfoliation and Peptide Adsorption on Si for AFM
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In sample preparation for AFM measurements, Si substrates were
first annealed on a hot plate at 200 °C for 30 min. After annealing,
graphite flakes were transferred to Si substrates using a mechanical
exfoliation method. 500-nM peptide solution was incubated for 1 h
at room temperature. After incubation, the solution was removed by
blowing with N2 gas.
The surface morphology of the
peptide was characterized by using an atomic force microscope (Agilent
5500 and Asylum Cypher) in air. The surface morphology was measured
in tapping mode (AC mode). The AFM instrument was equipped with a
silicon cantilever (OMCL-AC160TS-R3, Olympus, Japan) with a resonance
frequency of 300 kHz and a spring constant of 26 N/m.
first annealed on a hot plate at 200 °C for 30 min. After annealing,
graphite flakes were transferred to Si substrates using a mechanical
exfoliation method. 500-nM peptide solution was incubated for 1 h
at room temperature. After incubation, the solution was removed by
blowing with N2 gas.
The surface morphology of the
peptide was characterized by using an atomic force microscope (Agilent
5500 and Asylum Cypher) in air. The surface morphology was measured
in tapping mode (AC mode). The AFM instrument was equipped with a
silicon cantilever (OMCL-AC160TS-R3, Olympus, Japan) with a resonance
frequency of 300 kHz and a spring constant of 26 N/m.
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