Multimode scanning probe microscope

Manufactured by Digital Instruments

Sourced in United States

The Multimode Scanning Probe Microscope is a highly versatile instrument designed for high-resolution imaging and analysis of surface topography. It utilizes a probe to scan the surface of a sample, generating detailed three-dimensional representations of the sample's surface features. The instrument is capable of operating in various scanning modes, enabling users to capture a wide range of data and surface information.

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Lab products found in correlation

Nanoscope iiia controller, by Digital Instruments (2 mentions) Dimension 3100 scanning probe microscope, by Digital Instruments (2 mentions) Omcl ac160ts, by Olympus (2 mentions) Nanoscope 5 controller, by Digital Instruments (1 mentions) E scanner, by Veeco (1 mentions) Ti400, by Fluke (1 mentions) Feg 250, by Thermo Fisher Scientific (1 mentions) Raman spectrometer, by Renishaw (1 mentions) Ftir nicolet 6700, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Nanoscope IIIa Multimode scanning probe microscope

6 protocols using multimode scanning probe microscope

Tapping Mode AFM Imaging of Nanoscale Samples

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For AFM inspection, 40-μl sample aliquots were centrifuged at 1700 × g for 5 min using an Eppendorf 5417R centrifuge. The pellet was suspended in an equal volume of water, and a 10-μl aliquot was deposited on freshly cleaved mica and dried under mild vacuum. Tapping mode AFM images were acquired in air using a Dimension 3100 Scanning Probe Microscope equipped with a “G” scanning head (maximum scan size 100 μm) and driven by a Nanoscope IIIa controller, and a Multimode Scanning Probe Microscope equipped with “E” scanning head (maximum scan size 10 μm), driven by a Nanoscope V controller (Digital Instruments, Bruker). Single beam uncoated silicon cantilevers (type OMCL-AC160TS, Olympus) were used. The drive frequency varied between 280 and 330 kHz, the scan rate was between 0.4 and 0.7 Hz. Height and width of imaged objects were measured from the corresponding cross-section profiles in topographic AFM images. Widths at half-height were measured to correct tip size effects (20 (link)) and standard errors are reported. The object volume V was calculated from the equation,
where h is the imaged object height and a is its half-corrected width (20 (link)).

Natalello A., Mangione P.P., Giorgetti S., Porcari R., Marchese L., Zorzoli I., Relini A., Ami D., Faravelli G., Valli M., Stoppini M., Doglia S.M., Bellotti V, & Raimondi S. (2016). Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS. The Journal of Biological Chemistry, 291(18), 9678-9689.

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Characterization of Protein Aggregates by AFM and DLS

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The sample preparation, as well as AFM and DLS measurements have been described in detail in Giurleo et al. [11 (link)]. Below, we summarize them briefly.
AFM. The βLGa samples were imaged on mica surfaces by a MultiMode Scanning Probe Microscope (Digital Instruments, New York, NY, USA) with a TESP tip in tapping mode. To obtain better adhesion of protein aggregates to the mica surface, chemical surface modification with (3-aminopropyl) triethoxysilane was implemented, as described in Giurleo et al. [11 (link)].
DLS. Fluctuations of scattered light intensity were measured using a homodyne technique. Round borosilicate glass cuvettes (Kimble Glass, Düsseldorf, Germany) were used for all DLS measurements. For the DLS study (details in S-II), 250 μL of incubated sample was placed in a clean dry cuvette. Twenty correlation functions were measured sequentially for 30 s apiece for the incubated sample. The cuvette chamber was held at a constant temperature of 37 °C.

Acharjee M.C., Ledden B., Thomas B., He X., Messina T., Giurleo J., Talaga D, & Li J. (2023). Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor. Sensors (Basel, Switzerland), 24(1), 81.

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Atomic Force Microscopy of Amyloid Aggregation

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AFM measurements were performed at room temperature using scan rates between 1.0 and 1.5 Hz in the tapping mode on a MultiMode scanning probe microscope equipped with a Nano-Scope IIIa controller (Digital Instruments) using an E-scanner (scan size 15 mm-615 mm) and a MMMC cantilever holder (Veeco Instruments, Mannheim, Germany) equipped with a silicon SPM sensor (PPPNCHR, NanoAndMore, Wetzlar, Germany) as previously described^{62 (link)}. hIAPP (50 µM) without and with anle145c (10 µM) was incubated for various time intervals in 10 mM Tris-HCl, 150 mM NaCl buffer solution and then deposited on freshly cleaved mica. The samples were dried with a gentle stream of nitrogen, rinsed with water, dried again with a stream of nitrogen and finally freeze-dried overnight, as described previously^{61 (link)}. The dried samples were scanned in air with drive frequencies around 240 kHz and drive amplitudes between 15 and 379 mV. All height and amplitude images of sample regions were acquired with resolution of 5.1 Mpixels. For image analysis and processing, the software NanoScope version 5 (Veeco Instruments, Mannheim, Germany) was used.

Saravanan M.S., Ryazanov S., Leonov A., Nicolai J., Praest P., Giese A., Winter R., Khemtemourian L., Griesinger C, & Killian J.A. (2019). The small molecule inhibitor anle145c thermodynamically traps human islet amyloid peptide in the form of non-cytotoxic oligomers. Scientific Reports, 9, 19023.

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Comprehensive Multi-Technique Characterization of Composite Materials

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The samples were examined with a Quanta FEG250 field emission scanning electron microscopy (FE-SEM, FEI, USA) at an acceleration voltage of 20 kV. Samples were broken and the fractured surface were coated with a thin layer of gold powder to avoid the accumulation of charge and improve the conductivity, and a transmission electron microscopy JEM-2100 (TEM, Jeol, Japan), respectively, with an acceleration voltage of 200 kV. The samples were dispersed in ethanol using ultrasonic mixing for 15 min and some pieces were collected on 200 mesh carbon coated copper grids. Atomic force microscope (AFM) measurement was conducted on a multimode scanning probe microscope from Digital Instruments with NanoscopeIa controller. X-ray photoelectron spectroscopy (XPS) was carried out with Kratos AXIS ULTR DLD spectrometer. Fourier transform infrared (FTIR) spectra were obtained using a Nicolet 6700 FTIR (Thermal scientific Inc. USA) between 400 and 4000 cm⁻¹. Raman spectra were obtained by Raman spectrometer with laser wavelength of 532 nm (Renishaw plc, Wotton-under-Edge, UK). Thermal conductivities of the composites were determined with laser flash apparatus (LFA, Netzsch 447, Germany). The sample size for in-plane and out-of plane measurement was round with a diameter of 25.4 and 12.7 mm, respectively. The infrared (IR) photos were captured by IR camera (Fluke, Ti400, U.S.A.).

Wang T., Wang M., Fu L., Duan Z., Chen Y., Hou X., Wu Y., Li S., Guo L., Kang R., Jiang N, & Yu J. (2018). Enhanced Thermal Conductivity of Polyimide Composites with Boron Nitride Nanosheets. Scientific Reports, 8, 1557.

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Imaging Alpha-Synuclein Fibrils by AFM

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After a 500-fold dilution, 10 μl of α-Syn fibrils were finally deposited on freshly cleaved mica and dried under mild vacuum. Tapping mode AFM images were acquired in air using a Dimension 3100 Scanning Probe Microscope and a Multimode Scanning Probe Microscope (Digital Instruments, Bruker). Single beam uncoated silicon cantilevers (type OMCL-AC160TS; Olympus) were used. The drive frequency was between 290 and 310 kHz; the scan rate was between 0.4 and 0.5 Hz. Fibril height was measured from the cross-section height of topographic AFM images.

Porcari R., Proukakis C., Waudby C.A., Bolognesi B., Mangione P.P., Paton J.F., Mullin S., Cabrita L.D., Penco A., Relini A., Verona G., Vendruscolo M., Stoppini M., Tartaglia G.G., Camilloni C., Christodoulou J., Schapira A.H, & Bellotti V. (2014). The H50Q Mutation Induces a 10-fold Decrease in the Solubility of α-Synuclein. The Journal of Biological Chemistry, 290(4), 2395-2404.

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Characterizing Cellulose Nanofibers via AFM

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The CNF samples cast on bare mica
were imaged on a MultiMode scanning probe microscope (Digital Instruments,
Inc., USA) in the tapping mode using a cantilever with an 8 nm radius
spherical tip (spring constant of 40 N m^–1 and a
resonance frequency of ca. 260 kHz). Typically, images of size in
the range 5 μm × 5 μm, 2.5 μm × 2.5 μm,
or lower were obtained. From 512 to 1024 lines were taken per images.
Images were sampled at 1024–1536 points per lines that were
used in most cases to extract width and height features. The resolution
for CNFs’ width evaluation was evaluated to be 1.5–2.5
nm based on a half pixel contrast criterion with pixel shortest dimension
ranging from 3 to 5 nm. Five hundred CNFs were randomly selected to
individually obtain the width and height distributions. In order to
analyze the relationship between width and height, we selected 200
CNFs in a broad range of sizes.

Mattos B.D., Tardy B.L, & Rojas O.J. (2019). Accounting for Substrate Interactions in the Measurement of the Dimensions of Cellulose Nanofibrils. Biomacromolecules, 20(7), 2657-2665.

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