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Nova spm software

Manufactured by NT-MDT

Nova SPM software is a comprehensive scanning probe microscopy (SPM) data acquisition and analysis platform. It provides a user-friendly interface for controlling SPM instrumentation and processing the acquired data. The software supports a wide range of SPM techniques, including atomic force microscopy (AFM), scanning tunneling microscopy (STM), and other related methods. Nova SPM software enables researchers and scientists to efficiently collect, visualize, and analyze high-resolution surface information obtained from their SPM experiments.

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6 protocols using nova spm software

1

Visualizing Purified Proteins using TEM and AFM

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Purified proteins were examined in a transmission electron microscope, JEM 100CXII (JEOL, Tokyo, Japan). For atomic force microscopy, an Integra Prima microscope and Nova SPM software (NT-MDT, Moscow, Russia) were used. Scanning was performed in semicontact mode using a 35 nm gold cantilever, NSG01 (NT-MDT). The protein sample was applied to a sapphire substrate, coated with mica and dried at room temperature. PBS was used as a negative control.
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2

Structural Analysis of HEV-3 ORF2 Protein

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A total of 3 μL of purified HEV-3 ORF2 110–610_6his recombinant protein was adsorbed onto glow discharged Carbon-Formvar-coated copper grids for 60 s. The grids were then washed by floating on water droplets, followed by staining with 2% (w/v) uranyl acetate (UA) for 20 s. Particles were imaged using an FEI Tecnai G2 20 (FEI, Hillsboro, OR, USA) electron microscope operating at 200 kV. An Integra Prima microscope and Nova SPM software (NT-MDT, Moscow, Russia) were used for atomic force microscopy. Scanning was performed in semi-contact mode, using gold cantilever NSG01 (NT-MDT). The protein sample was applied to a sapphire substrate coated with mica and dried at room temperature. PBS was used as a negative control. Cryo-EM grids were prepared as described by Byrne et al., 2019 [49 (link)].
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3

Characterization of Recombinant Protein Particles

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The particles formed by the recombinant protein after refolding were examined using a transmission electron microscope and atomic force microscope. Electron microscopy was performed on a JEM 1400 instrument (JEOL, Tokyo, Japan). The 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. Particle sizes (n = 20) in digital photographs were determined using the ImageJ software [62 (link)].
Atomic force microscopy was performed using an Integra Prima microscope and Nova SPM software (NT-MDT, Moscow, Russia). The scanning was performed in the semi-contact mode using gold cantilever NSG01 (NT-MDT). Particle sizes (n = 20) were determined using the NT-MDT Nova v. 1.06.26 software supplied with the instrument.
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4

Quantitative Surface Morphology Analysis

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The quantitative analysis of the surface morphology of the uncoated and HA-coated substrates was performed with a Solver P47-PRO (NT-MDT, Moscow, Russia) atomic force microscope (AFM) using triangular golden silicon probes (NT-NDT) with a typical spring constant of 28 N· m1 and a resonance frequency of 420 kHz. All of the images were collected in contact AFM mode in air at a typical frequency of 1.5 Hz with an image resolution of 256 points per line. Squares of different sizes (5 × 5 μm2 and 35 × 35 μm2 ) were scanned, and the Nova SPM software (NT-MDT, Moscow, Russia) was used to analyse the surface roughness. Three different 3D parameters were used to characterize the surface roughness: (Sa), which is the arithmetic mean of the absolute values of the surface departure from the mean plane in the samples area; the root mean square roughness (Sq), which is an index used to represent the standard deviation of the surface heights; and Sdr, which is the developed interfacial area ratio.
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5

Multimodal Characterization of Purified Proteins

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Analysis of particle size by dynamic light scattering method was performed using a Zetasizer NanoS90 particle size analyzer (Malvern).
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.
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6

Microscopic Analysis of Virus-Like Particles

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Virus-like particles were examined in transmission electron microscope JEOL LEM 1011. For atomic force microscopy an Integra Prima microscope and Nova SPM software (NT-MDT, Russia) were used. The scanning was performed in semi contact mode using gold cantilever NSG01 (NT-MDT). The protein sample was applied to a sapphire substrate coated with mica and dried at room temperature. PBS was used as a negative control.
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