Fastscan d

Manufactured by Bruker

Sourced in United States

The FastScan D is a high-speed atomic force microscope (AFM) designed for rapid, high-resolution imaging of samples. The instrument can capture images at a rate of up to 12 frames per second, enabling real-time observation of dynamic processes. The FastScan D utilizes specialized cantilever technology and advanced control electronics to achieve this high-speed performance.

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Lab products found in correlation

Dimension fastscan bio afm, by Bruker (3 mentions) Nanowizard 3, by Bruker (2 mentions) Nanoscope iiia controller, by Digital Instruments (1 mentions) J scanner, by Bruker (1 mentions) Dimension fastscan, by Bruker (1 mentions) Hplc grade water, by Merck Group (1 mentions) Dimension fastscan afm, by Bruker (1 mentions) Tespa probe, by Bruker (1 mentions) Jpk nanowizard 4 afm, by Bruker (1 mentions)

9 protocols using fastscan d

Custom AFM Imaging Protocols

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All imaging was performed on a home-built atomic force microscope, based on the Bruker MultiMode. A custom-built drop-in replacement for the original microscope head, providing the means to use small cantilevers and photothermal excitation, was used and is described in detail elsewhere [28 (link),29 (link),30 (link),47 (link)].
All imaging was done with either Olympus AC10DS (for thrombocytes) or Bruker FastScan-D cantilevers (for bacterial imaging). PORT amplitudes used were between 25 and 120 nm, with typical setpoints between 0.5 and 5 nm, corresponding roughly to between 50 and 2000 pN.
PORT for platelet and E. coli imaging was implemented using a Nanoscope 5 controller with a modified PeakForce-HR workspace that allows splitting the modulation from the z-signal. A custom-built scaling and offset circuit was used to adapt output voltage levels as required by the head electronics. B. subtilis imaging was performed using home-built AFM software based on a standalone FPGA (USB-7856R OEM, National Instruments, Austin TX, USA), with software and hardware programming as described elsewhere [30 (link)], and using the amplifiers in a modified Nanoscope-IIIa controller (Digital Instruments, Santa Barbara, CA, USA) that allow for input of external low-voltage scan signals. All images were acquired on a J-scanner (Bruker, Santa Barbara CA, USA) (120 × 120 × 5.2

μ

m range).

Nievergelt A.P., Brillard C., Eskandarian H.A., McKinney J.D, & Fantner G.E. (2018). Photothermal Off-Resonance Tapping for Rapid and Gentle Atomic Force Imaging of Live Cells. International Journal of Molecular Sciences, 19(10), 2984.

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Optimizing AFM Imaging Parameters

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AFM was performed under the described aqueous buffers using a Dimension FastScan and FastScan D type probes (Bruker Nano Surfaces Division). Parameters were optimized whilst imaging to minimize applied forces, at low tapping amplitudes and moderate gains, typically scanning at 1–4 Hz and 1024 × 1024 pix. Topographs were processed and analysed using Nanoscope Analysis software (v1.8).

Adams P.G., Vasilev C., Hunter C.N, & Johnson M.P. (2018). Correlated fluorescence quenching and topographic mapping of Light-Harvesting Complex II within surface-assembled aggregates and lipid bilayers. Biochimica et Biophysica Acta, 1859(10), 1075-1085.

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AFM Imaging of Hydrated Samples

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All AFM imaging was carried out at room temperature with the samples hydrated in imaging buffer. Data were recorded using a Dimension FastScan Bio AFM (Bruker, Santa Barbara, USA), using force–distance-curve based imaging (PeakForce Tapping mode). Force–distance curves were recorded over 10–40 nm (PeakForce Tapping amplitude of 5–20 nm), at a frequency of 8 kHz. FastScan D (Bruker) cantilevers were used for all imaging (resonance frequency of ∼110 kHz, nominal spring constant ∼0.25 Nm^–1). Images were processed using first-order line-by-line flattening, median line-by-line flattening and zeroth order plane fitting to remove the sample tilt and background using Gwyddion.

Akpinar B., Haynes P.J., Bell N.A., Brunner K., Pyne A.L, & Hoogenboom B.W. (2019). PEGylated surfaces for the study of DNA–protein interactions by atomic force microscopy †Electronic supplementary information (ESI) available. See DOI: 10.1039/c9nr07104k. Nanoscale, 11(42), 20072-20080.

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High-Resolution Atomic Force Microscopy

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AFM was performed in intermittent-contact mode on a Nanowizard III AFM with an UltraSpeed head (JPK, Germany; now Bruker AXS, CA, USA) using a FastScanD (Bruker AXS, CA, USA) cantilever with 0.25 N m^–1 spring constant and 120 kHz resonance frequency. Images were acquired with a drive frequency of 90–110 kHz and an amplitude of 9–15 nm, representing an approximately 30–40% drop from the free amplitude 5–10 μm above the sample surface. All AFM was performed in liquid in HEPES buffer and was performed within 3 hours of immobilising. Images are 512 × 512 pixels (unless otherwise specified) with an aspect ratio of 1 : 1. 5 × 5 μm² scans were performed at a line frequency of 1 Hz, 500 × 500 nm² and 350 × 350 nm² scans were performed at 3–5 Hz. Data was analysed in Gwyddion 2.52 (; http://gwyddion.net/).27 5 × 5 μm² scans were processed by applying a first-order plane fit. A first-order plane fit, followed by line-by-line 2^nd order flattening and a Gaussian filter with σ = 1 pixel, to remove high-frequency noise, was applied to 500 × 500 nm² and 350 × 350 nm² scans.

Benn G., Pyne A.L., Ryadnov M.G, & Hoogenboom B.W. (2019). Imaging live bacteria at the nanoscale: comparison of immobilisation strategies. The Analyst, 144(23), 6944-6952.

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Atomic Force Microscopy Imaging of Exosporium

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A suspension of exosporium fragments (Section 2.4) was incubated on freshly cleaved mica (Agar Scientific) for 20 min, then washed with 10 × 1 ml of HPLC grade water (Sigma Aldrich). Samples imaged in water were used without further preparation; samples imaged in air were blown dry with filtered nitrogen. Imaging in water was performed using a Dimension FastScan AFM (Bruker) and FastScan D probes (nominal force constant and resonant frequency 0.25 N/m and 110 kHz in water, respectively) in tapping mode with a free amplitude of approximately 1.2 nm and a set point of 80–90% of this value. Imaging in air was performed using a Multimode (Bruker) or NanoWizard^® 3 (JPK) AFM in tapping mode using TESPA probes (Bruker) with a nominal force constant and resonant frequency of 40 N/m and 320 kHz, respectively. The free amplitude was approximately 8 nm and images were acquired with a set point 90–95%. In both environments, the feedback gains, scan rate, set point and Z range were adjusted for optimal image quality while scanning. Height and phase images were acquired simultaneously and processed (cropping, flattening, plane fitting) using NanoScope Analysis or JPK DP software.

Janganan T.K., Mullin N., Tzokov S.B., Stringer S., Fagan R.P., Hobbs J.K., Moir A, & Bullough P.A. (2016). Characterization of the spore surface and exosporium proteins of Clostridium sporogenes; implications for Clostridium botulinum group I strains. Food Microbiology, 59, 205-212.

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Atomic Force Microscopy of NuPODs

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All
AFM measurements were performed at
room temperature in liquid. Images were obtained using a Dimension
FastScan Bio AFM (Bruker) operated in Tapping mode. FastScan D (Bruker)
cantilevers were used for all imaging with a resonance frequency of
∼110 kHz, measured spring constant of ∼0.15 N m^–1, and quality factor of ∼2 in water. The force
applied to the sample was minimized by setting the highest possible
amplitude set-point voltage, which was typically above 85% of free
oscillation close to the sample surface. Single line scanning experiments
provided an enhanced time resolution while minimizing disturbance
to the NuPODs. For these experiments, a single NuPOD was centered
and the frame size decreased to 120 nm before disabling the slow-scan
axis over the center of the pore. Where possible, data were collected
at 5, 10, and 20 Hz for each pore imaged.

Stanley G.J., Akpinar B., Shen Q., Fisher P.D., Lusk C.P., Lin C, & Hoogenboom B.W. (2019). Quantification of Biomolecular Dynamics Inside Real and Synthetic Nuclear Pore Complexes Using Time-Resolved Atomic Force Microscopy. ACS Nano, 13(7), 7949-7956.

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Nuclear Pore Complex Dynamics Analyzed by AFM

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All
AFM measurements were performed at
room temperature in import buffer (20 mM Hepes, 110 mM CH₃COOK, 5 mM Mg(H₃COO)₂, 0.5 mM EGTA, pH 7.4).
Kymographs were obtained using a Dimension FastScan Bio AFM (Bruker),
using tapping mode AFM. FastScan D (Bruker) cantilevers were used
for all experiments, and the applied force was minimized (optimized)
as described for the NuPODs. Images of the nuclear envelope were recorded
to ascertain if the AFM tip probed the cytoplasmic or nucleoplasmic
face of the nuclear envelope.^{17 (link)} A 300 ×
300 nm image at 304 samples/line of a single NPC was recorded; this
ensured capture of background nuclear envelope as well as the NPC.
When the position along the slow-scan axis was at the center of the
NPC (see Figure 1A,B,
AFM images, white-dashed lines), the slow scan-axis movement was disabled.
A kymograph was then produced with height in the fast-scan axis and
time in the slow-scan axis. The line rate was set to 5, 10, or 20
Hz, and the gains were optimized to best track the contours of the
sample.

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Atomic Force Microscopy Tapping Mode

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All AFM measurements were performed using a JPK Nanowizard 4 AFM (Bruker, Berlin, Germany). Images were acquired in tapping mode by using cantilevers (FastScan D, Bruker) with a normal spring constant of ~0.25 N/m, and a resonant frequency of ~110 kHZ in liquid. The sensitivity of cantilevers was measured on mica and the spring constant were calibrated by using thermal tune methods^{53 (link)}. Force-distance curves were acquired at 500 nm/s.

Falzone M.E., Feng Z., Alvarenga O.E., Pan Y., Lee B., Cheng X., Fortea E., Scheuring S, & Accardi A. (2022). TMEM16 scramblases thin the membrane to enable lipid scrambling. Nature Communications, 13, 2604.

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Visualizing SNARE Complex Formation Using AFM

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Purified v-SNARE nanodiscs and t-SNARE liposomes were suspended in HBS (100 mM NaCl and 50 mM HEPES, pH 7.5) containing 1 mM CaCl₂, and 45 μl of the sample was deposited onto freshly-cleaved mica (10 mm diameter discs). After a 5-min adsorption period, the sample was rinsed with the same buffer solution to remove unabsorbed material. AFM imaging was carried out with a Dimension FastScan Bio AFM. All samples were imaged in tapping mode (in fluid) with silicon nitride probes (FastScan D, Bruker AFM Probes). These cantilevers had a spring constant of ~0.25 N/m and a drive frequency of ~85 kHz (10–20% below the resonance frequency). The applied imaging force was kept as low as possible (A_S/A₀~0.85). Images were captured at a scan rate of 20 Hz, with 512 scan lines per area. Data analysis was performed with Gwyddion 2.40. Nanodisc diameter was determined by drawing cross-sections of the imaged structures.

Bao H., Goldschen-Ohm M., Jeggle P., Chanda B., Edwardson J.M, & Chapman E.R. (2015). Exocytotic fusion pores are composed of both lipids and proteins. Nature structural & molecular biology, 23(1), 67-73.

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