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Integra prima microscope

Manufactured by NT-MDT
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The Integra Prima is a multi-purpose atomic force microscope (AFM) designed for a wide range of applications. It features a modular architecture and can be equipped with various modules to enable various imaging and spectroscopy modes. The Integra Prima provides high-resolution imaging and analysis capabilities for researchers and scientists.

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Lab products found in correlation

Nova spm software, by NT-MDT (5 mentions) Nsg01, by NT-MDT (3 mentions) Gold cantilever nsg01, by NT-MDT (2 mentions) Carbon formvar coated copper grids, by Ted Pella (2 mentions) Jem 100cx 2, by JEOL (1 mentions) Tecnai g2 20, by Thermo Fisher Scientific (1 mentions) Jem 1400, by JEOL (1 mentions) Jem 1400 instrument, by JEOL (1 mentions)

5 protocols using integra prima microscope

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.
Zykova A.A., Blokhina E.A., Kotlyarov R.Y., Stepanova L.A., Tsybalova L.M., Kuprianov V.V, & Ravin N.V. (2020). Highly Immunogenic Nanoparticles Based on a Fusion Protein Comprising the M2e of Influenza A Virus and a Lipopeptide. Viruses, 12(10), 1133.
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2

Structural Analysis of HEV-3 ORF2 Protein

Cited 1 time
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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)].
Takova K., Koynarski T., Minkov G., Toneva V., Mardanova E., Ravin N., Lukov G.L, & Zahmanova G. (2021). Development and Optimization of an Enzyme Immunoassay to Detect Serum Antibodies against the Hepatitis E Virus in Pigs, Using Plant-Derived ORF2 Recombinant Protein. Vaccines, 9(9), 991.
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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.
Blokhina E.A., Mardanova E.S., Zykova A.A., Stepanova L.A., Shuklina M.A., Tsybalova L.M, & Ravin N.V. (2023). Plant-Produced Nanoparticles Based on Artificial Self-Assembling Peptide Bearing the Influenza M2e Epitope. Plants, 12(11), 2228.
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4

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.
Mardanova E.S., Kotlyarov R.Y., Stuchinskaya M.D., Nikolaeva L.I., Zahmanova G, & Ravin N.V. (2022). High-Yield Production of Chimeric Hepatitis E Virus-Like Particles Bearing the M2e Influenza Epitope and Receptor Binding Domain of SARS-CoV-2 in Plants Using Viral Vectors. International Journal of Molecular Sciences, 23(24), 15684.
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5

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.
Mardanova E.S., Takova K.H., Toneva V.T., Zahmanova G.G., Tsybalova L.M, & Ravin N.V. (2020). A plant-based transient expression system for the rapid production of highly immunogenic Hepatitis E virus-like particles. Biotechnology letters, 42(11).
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