Ppp nchr tips

Manufactured by Nanosensors

The PPP-NCHR tips are a type of lab equipment designed for use with Atomic Force Microscopy (AFM) instruments. They feature a high-aspect-ratio nano-scale probe intended for high-resolution imaging and measurement applications.

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Lab products found in correlation

D5000 diffractometer, by Siemens (1 mentions) Nx 10, by Nanosensors (1 mentions) Nx10 instrument, by Park Systems (1 mentions)

5 protocols using ppp nchr tips

Structural Characterization of Thin Films

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Optical microscope pictures were taken using an Olympus BX51 equipped with polarizer and analyzer.
X-ray diffraction measurements were carried out with a Siemens D-5000 diffractometer.
AFM images were obtained using a Park NX10 system using PPP-NCHR tips (Nanosensors) in noncontact mode and applying adaptive scan rate to slow down scan speed at crystallite borders. Subsequent data analysis was done using the Gwyddion software. In order to calculate the grain sizes, a dedicated Gwyddion tool has been used. In particular, setting a height threshold value, this tool can recognize different grains laying in the same thin film.

Temiño I., Basiricò L., Fratelli I., Tamayo A., Ciavatti A., Mas-Torrent M, & Fraboni B. (2020). Morphology and mobility as tools to control and unprecedentedly enhance X-ray sensitivity in organic thin-films. Nature Communications, 11, 2136.

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Atomic Force Microscopy of Crystallites

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AFM measurements are performed using a Park NX10 system using PPP‐NCHR tips (Nanosensors) in noncontact mode and applying adaptive scan‐rate to slow down scan speed at crystallite borders. AFM images were processed through Gwyddion software.

Basiricò L., Fratelli I., Verdi M., Ciavatti A., Barba L., Cesarini O., Bais G., Polentarutti M., Chiari M, & Fraboni B. (2022). Mixed 3D–2D Perovskite Flexible Films for the Direct Detection of 5 MeV Protons. Advanced Science, 10(1), 2204815.

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AFM Characterization of Crystallite Surfaces

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AFM measurements are performed on a Park NX10 system using PPP-NCHR tips (Nanosensors) in non-contact mode and applying adaptive scan-rate to slow down scan speed at crystallite borders.

Basiricò L., Ciavatti A., Cramer T., Cosseddu P., Bonfiglio A, & Fraboni B. (2016). Direct X-ray photoconversion in flexible organic thin film devices operated below 1 V. Nature Communications, 7, 13063.

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Mature Fibril Preparation for AFM

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Mature fibril samples were obtained from the end points of the ThT assay. Each fibril sample (20 μL) was coated onto freshly cleaved mica (Ted Pella Inc., Redding, CA) and incubated for 15 minutes. The mica surface was then washed with water (200 μL) three times to remove any un-adsorbed protein species and salt, and air-dried for 1 hour before imaging. All AFM images were obtained with a Park Systems NX-10 (Suwon, South Korea) using PPP-NCHR tips (Nanosensors, Neuchatel, Switzerland).

Williams J.K., Yang X., Atieh T.B., Olson M.P., Khare S.D, & Baum J. (2018). Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein. Journal of molecular biology, 430(16), 2360-2371.

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Collagen Fibril Self-Assembly on Mica

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Type I collagen from rat tail (Discovery Labware Inc., Bedford, MA) was diluted in 10 mM phosphate buffered saline (PBS) pH 7.4 to a final concentration of 2.0 mg/mL and incubated at 37 °C for 2 hours for fibril self-assembly. A sample volume of 20 μL was deposited on a 1 cm × 1 cm square of freshly cleaved mica (Ted Pella Inc., Redding, CA) and incubated at room temperature for 15 min. Then the surface of the sample was washed with 1 mL of deionized water and left to dry at room temperature for 1 h before being imaged. The samples were imaged by an NX-10 instrument (Park Systems, Suwon, South Korea) in non-contact mode with PPP-NCHR tips (nominal force constant 42 N/m; 330 kHz frequency; Nanosensors, Neuchatel, Switzerland). Images were not filtered and minimal processing was conducted using XEI (Park Systems, Suwon, South Korea).

Zhu J., Hoop C.L., Case D.A, & Baum J. (2018). Cryptic binding sites become accessible through surface reconstruction of the type I collagen fibril. Scientific Reports, 8, 16646.

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