Nsg01
The NSG01 is a scanning probe microscope (SPM) designed for high-resolution imaging and analysis of surfaces at the nanoscale. It is capable of operating in various SPM modes, including atomic force microscopy (AFM) and scanning tunneling microscopy (STM), to provide detailed topographical and electronic information about the sample.
Lab products found in correlation
20 protocols using nsg01
Nanocellulose Morphology Characterization by AFM
Atomic Force Microscopy of PLGA Nanoformulations
Atomic Force Microscopy of Amyloid Fibrils
Atomic Force Microscopy of Amyloid Fibrils
Microparticle Characterization via AFM
were analyzed and characterized using the atomic force microscope
(NT-MDT Solver Pro microscope, NT-MDT Spectrum Instruments, Zelenograd,
Moscow, RU), with a single-crystal silicon–antimony-doped probe
and a gold-coated base (NSG-01 from NT-MDT). To reduce nonlinearity
and hysteresis in the measurements, prior to the AFM analyses the
microscope was calibrated by a calibration grid (TGQ1 from NT-MDT).
The analyses were performed using the tapping mode where the cantilever
is driven to oscillate vertically near its resonance frequency. The
lyophilized sample was resuspended in Milli-Q water, deposited on
a mica substrate, and dried under a flux of argon. All the data were
collected using the software Nova (NT-MDT). The resolution of the
images acquired was 15 nm.
Reversible Surface Wrinkles in PEDOT:PSS
Multimodal Characterization of Purified Proteins
Atomic force microscopy was performed using an Integra Prima microscope and Nova SPM software (NT-MDT, Moscow, Russia). The scanning was performed in semi contact mode using gold cantilever NSG01 (NT-MDT).
Electron microscopy was performed on a JEM 1400 instrument (JEOL, Tokyo, Japan). Purified proteins were placed on carbon-formvar-coated copper grids (TED PELLA, Redding, CA, USA) and stained with 1% (w/v) uranyl acetate in methanol. The average size of the particles was determined using 10 particles.
Quantitative Surface Characterization of Dried Films
Atomic Force Microscopy of Protein Aggregates
Electrochemical Characterization of TIECP Films
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