Ecell = 4F(ΔZ)(1 − ηcell2)/3(ΔZ1.5)tan θ, where Ecell: Young’s modulus; F: loading force; ηcell: Poisson ratio; ΔZ: indentation; θ: tip half cone opening angle.
Picoview software
PicoView is a software package developed by Agilent Technologies for controlling and analyzing data from their atomic force microscopes (AFMs). It provides a user-friendly interface for setting up and running AFM experiments, as well as tools for processing and visualizing the acquired data.
Lab products found in correlation
8 protocols using picoview software
Measuring Cellular Biomechanics with AFM
Atomic Force Microscopy of Chondrocyte-Derived Extracellular Vesicles
Atomic Force Microscopy Imaging of Lysozyme Fibrils
study, the solutions
of lyz fibrils were diluted to 100-fold with water. Then, around 5
μL of this sample solution was adsorbed onto a freshly cleaved
muscovite ruby mica sheet (ASTM VI grade Ruby Mica from Micafab, Chennai,
India). Thereafter, the mica sheet was dried for 30 min in vacuum
in an inert atmosphere. The complexes were incubated for 15 min prior
to adsorption onto the mica sheet. AFM was performed in the AAC mode
on PicoPlus 5500 ILM AFM (Agilent Technologies, USA), which was attached
with a piezo-scanner of a maximum range of 9 μm. Here, microfabricated
silicon cantilevers of NANOSENSORS (USA) were used. The resonance
frequency of the cantilever oscillation was 146–236 kHz, whereas
the force constant was 21–98 N/m. The rate of the scan speed
was 0.5 lines/s while taking the images (256 by 256 pixels). All the
images were processed by flattening using PicoView software (Agilent
Technologies, 1.1 version), whereas their manipulation was conducted
by Pico Image Advanced version software.
AFM Characterization of Cells and Collagen I Gel
Atomic Force Microscopy of Polymer-DNA Complexes
Agilent 5500 microscope without pretreatment of the sample. To take
the images of polymer–DNA complexes, the contact mode in air
was conducted on mica. The microfabricated Si-type NCH cantilevers
had a nominal spring constant of 0.2 N/m and a nominal resonance frequency
of 13 kHz. The scan rate employed was below 2 Hz to obtain good tracking
of the surface morphology. The polymer–DNA complexes were prepared
at Z+/– = 1 and kept at two different
temperatures 25 and 40 °C for 30 min, and then, a drop of the
sample solution was allowed to settle on the mica for 5 min. The samples
were air-dried overnight at respective temperatures. The images were
further autoflattened and analyzed using Agilent PicoView software.
Atomic Force Microscopy of Plastoglobules
Images were recorded at 1 ln/s and resolution 512 × 512, with minimal possible force applied. Surface probing for elasticity determination was done with a built-in plugin for PicoView software, recording and analysing force-distance curves. Usually, a resolution of 32 × 32 was used for probing a chosen region of approximately 2 μm × 2 μm. Images were processed with Gwyddion 2.49 software [79 (link),80 (link)].
Atomic Force Microscopy of Membrane Vesicles
Characterizing Thin Film Morphology and Composition
amplitude micrographs were obtained in tapping mode using a Pico Plus
AFM instrument (Molecular Imaging) with aluminum-coated silicon tips
(BudgetSensors) and a spring constant of 40 N m–1. A sample area of 3 μm by 3 μm was scanned at a rate
of 1 Hz while collecting data in topographic, phase, and amplitude
modes. Morphological changes are captured in micrographs using PicoView
software (Agilent) and postprocessed using Gwyddion.30 (link)FTIR imaging was performed with a Nicolet iN10 infrared
microscope (Thermo Scientific) after mounting the optical windows
on a motorized stage for scanning the infrared map in an XY pattern. OMNIC Picta software (Thermo Scientific) was utilized for
FTIR microscopy and spectral mapping. Individual spectra corresponding
to an average of 64 scans were collected over the range of 800–4000
cm–1 with 4 cm–1 resolution. All
samples were background-subtracted using an empty optical window.
Control experiments ensured that films exposed to humid air in the
absence of O3(g) correspond to the spectral features of
catechol despite any loss by sublimation, which was carefully monitored
to remain below 5%. Data processing to obtain the CD line (or corrected
peak heights after local baseline correction) was performed10 (link) to collect kinetic data from the average of
duplicate experiments with error bars corresponding to one standard
deviation.
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