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Snl 10 cantilevers

Manufactured by Bruker
Sourced in Germany

The SNL-10 cantilevers are a type of atomic force microscopy (AFM) probe. They are designed for high-resolution imaging and force measurement applications. The SNL-10 cantilevers feature a silicon nitride (Si3N4) material and have a nominal spring constant of 0.32 N/m. The cantilever's dimensions and specifications are optimized for stable and sensitive operation in various AFM modes.

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7 protocols using snl 10 cantilevers

1

Agarose-Coated Coverslip AFM Imaging

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AFM images of agarose-coated coverslips were acquired in liquid solution using a Nanoscope 5 Multimode-8 AFM system with SNL-10 cantilevers (Bruker) in tapping mode.
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2

Atomic Force Microscopy of Biomolecules

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20 μl of each sample, supplemented with 2 μl 10 mM HCl were deposited on a mica surface for 30 minutes and washed 5 times with 200 μl deionized water before being dried overnight at room temperature. AFM imaging was performed on a BioScope Catalyst atomic force microscope (Bruker), in peak force tapping mode in air. Resolution was set at 512 × 512 pixels, scan rate was 0.51 Hz, and scan sizes were 2 × 2 and 5 × 5 μm. Bruker SNL10 cantilevers were used for all measurements.
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3

Nucleosome Deposition and Atomic Force Microscopy

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For surface deposition, nucleosome samples were diluted with TCS buffer to a final concentration of 2 nM. 50 µL of diluted samples were pipetted onto APTES-modified mica (Grade V, SPI). Samples were then incubated at room temperature for 5 min. The mica discs were then rinsed with purified 18.2-MΩ deionized water. For samples intended for AFM imaging in air, the washed mica disks were then dried using a gentle N2 gas flow, perpendicular to the mica surface. For samples intended for imaging in liquid, the rinsed mica disks were quickly exchanged into imaging buffer (10 mM Tris-HCl pH 7.5, 3 mM NiCl2). All samples were imaged by AFM immediately following preparation. Data acquisition was performed using a MFP-3D AFM or a Cypher ES Environmental Atomic-Force Microscope (Asylum Research). The samples were imaged in tapping mode using a commercial silicon cantilever with a spring constant of 46 N/m. For air imaging, Asylum AC240 cantilevers were used; for liquid imaging, Bruker SNL-10 cantilevers were used. Images were captured at 512×512 pixels in the trace direction, at a scan size of 2 µm and a scan rate of 1.0 Hz. Image processing was carried out using publicly available software (Gwyddion).
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4

Nucleosome Deposition and Atomic Force Microscopy

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For surface deposition, nucleosome samples were diluted with TCS buffer to a final concentration of 2 nM. 50 µL of diluted samples were pipetted onto APTES-modified mica (Grade V, SPI). Samples were then incubated at room temperature for 5 min. The mica discs were then rinsed with purified 18.2-MΩ deionized water. For samples intended for AFM imaging in air, the washed mica disks were then dried using a gentle N2 gas flow, perpendicular to the mica surface. For samples intended for imaging in liquid, the rinsed mica disks were quickly exchanged into imaging buffer (10 mM Tris-HCl pH 7.5, 3 mM NiCl2). All samples were imaged by AFM immediately following preparation. Data acquisition was performed using a MFP-3D AFM or a Cypher ES Environmental Atomic-Force Microscope (Asylum Research). The samples were imaged in tapping mode using a commercial silicon cantilever with a spring constant of 46 N/m. For air imaging, Asylum AC240 cantilevers were used; for liquid imaging, Bruker SNL-10 cantilevers were used. Images were captured at 512×512 pixels in the trace direction, at a scan size of 2 µm and a scan rate of 1.0 Hz. Image processing was carried out using publicly available software (Gwyddion).
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5

Peptide Sample Preparation and AFM Imaging

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For AFM imaging, the peptides were suspended in a buffer containing 300 mM KCl and 10 mM HEPES (pH 7.4) to 1 μM final concentration, vortexed for 30 s, deposited on freshly cleaved mica, incubated for ~10 min, washed 3 times with the same (imaging) buffer, and scanned. To prepare peptide/lipid samples for AFM imaging, the lipids were suspended in the imaging buffer supplemented with 3 mM CaCl2 and bath-sonicated to obtain unilamellar vesicles. The peptide was added at 1:1000 or 1:500 peptide-to-lipid molar ratio followed by a ~ 1 min bath-sonication. The sample was drop-casted on the freshly cleaved mica surface and incubated for 20 min at room temperature, washed 3 times with the imaging buffer and the formed supported lipid bilayers were imaged in the same buffer. AFM imaging was performed on a Multimode AFM (Bruker) controlled by a Nanoscope V controller and the images were collected in PeakForce Tapping mode with SNL-10 cantilevers (Bruker). The images were analyzed using a Nanoscope Analysis v1.5 software or the SPM analysis package Gwyddion. All images were line flattened and color scale adjusted. For generating particle height histograms, the “Particle Analysis” feature in Nanoscope Analysis was used.
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6

DON characterization via AFM imaging

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For DON characterization via
atomic force microscopy (AFM), 112.5 fmol of DON sample was incubated
with a 3-fold molar excess of anti-DNP IgG in regard to DNP-binding
sites present on the DON for 30 min at room temperature. Afterward,
the reaction mixture was diluted to a final concentration of 3 nM
DON using TeMg12.5 mM buffer (20 mM Tris base, 1 mM
EDTA, 12.5 mM MgCl2, pH 7.6) and 5 μL was added on a freshly
cleaved mica disc (Plano GmbH) for 3 min at room temperature. Afterward,
10 μL of TeMg12.5 mM buffer was added on top
and DON were imaged in liquid using SNL-10 cantilevers (k = 0.35 N m–1, r = 2 nm, Bruker)
and tapping mode on a MultiModeTM 8 atomic force microscope (Bruker)
equipped with a NanoScope V controller. The obtained images were analyzed
using the NanoScope Analysis software (Bruker).
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7

Topographic Analysis of Dendrimer Surfaces

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Topographic profiles of the dendrimer-coated surfaces were characterized using a NanoWizard 3 AFM (JPK, Instruments AG, Berlin, Germany) in tapping mode at 293 K. The measurements in air were performed using NCHV-A cantilevers with a spring constant of k = 42 N m−1 and a tip radius of r < 8 nm, while the measurements in buffer were carried out with SNL-10 cantilevers with a spring constant of k = 0.35 N m−1 and a tip radius of r < 12 nm (Bruker, Karlsruhe, Germany).
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