The UV-vis spectra of the FL-MoS2 suspensions were recorded on a UV-1800PC spectrometer (Shanghai Mapada), and a quartz cell with a path length of 1.0 cm was used as the sample pool. The SEM images were obtained using a JEOL JSM-7500F scanning electron microscope, with an Au film coating (20 mA for 50 s) before SEM observation. The TEM images were measured using a field-emission transmission electron microscope (JEOL, JEM-2100) with an accelerating voltage of 200 kV. The Raman spectra were obtained using a Raman spectrometer (LabRAM HR Evolution, HORIBA JobinYvon, France) at 525 nm, and the powder samples were prepared on a SiO2/Si substrate. The X-ray diffraction (XRD) patterns were recorded on an XD-3 X-ray diffractometer (Beijing Purkinje General Instrument Co., Ltd., China) with a Cu Kα irradiation (λ = 0.15406 nm). The Fourier transformed infrared (FT-IR) spectra were recorded on a Bruker-Equinox 55 spectrometer in a transmittance mode in a wavenumber range of 4000 to 400 cm−1. The atomic force microscopy (AFM) measurement was performed on a Bruker NanoScope V instrument in a tapping mode. The N2 adsorption-desorption isotherms were obtained on a Surface Area and Porosity Analyzer (ASAP 2460, Micromeritics).
Nanoscope 5 instrument
Manufactured by Bruker
The NanoScope V is a high-resolution atomic force microscope (AFM) instrument designed for advanced nanoscale imaging, measurement, and characterization. It provides precise topographical and material property data with subnanometer resolution.
Automatically generated - may contain errors
2 protocols using nanoscope 5 instrument
1
Comprehensive Characterization of Fluorescent MoS2
2
Atomic Force Microscopy of Protein-DNA Complexes
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DNA and proteins were extensively dialyzed against sample deposition buffer (10 mM triethanolamine-HCl pH = 7.4, 150 mM NaCl, 1 mM MgCl2 and 1 mM DTT). For analysis of 2434 bp DNA, 3.71 fmol (0.3 ng/μl) DNA were incubated with varying amounts of Mst77F and control proteins (4-, 20- and 100-fold molar excess of protein over DNA) in a total volume of 20 μl at RT for 30 min. Samples were deposited on mica (Plano), incubated for 10 min and washed with 2 ml of ddH2O. For analysis of 12 bp random DNA, 0.04 μM were incubated with 0.04 or 0.64 μM Mst77F in a final volume of 50 μl. After 1:10 dilution in deposition buffer aliquots of 20 μl were pipetted onto mica and processed as before. Prior to imaging samples were dried for 20 min in a stream of filtered compressed air. Images of the different protein-DNA complexes were recorded on a Nanoscope V instrument (Bruker) using tapping mode in air and a NSC15/no Al cantilever (μMasch, resonance frequency of 325 kHz and force constant of 40 N/m). Scans were recorded at a rate of 0.996 Hz with a resolution of 512 × 512 pixels. Post-imaging flattening of data files was conducted with the Nanoscope software.
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