Single Particle Cryo-EM for Coronavirus-like Particle

Because viral particles are generally small (between tens and hundreds of nanometers in diameter), the traditional optical microscope is difficult to meet the needs of their morphological observation, which makes high-resolution electron microscopy (EM) an important means of current virology research. It can be utilized to study the structure and surface composition of viral particles, and the viral structure information with the near-atomic resolution is useful in the discovery and design of vaccines and antiviral drugs. Leveraging advanced cryo-electron microscopy (cryo-EM) imaging platform and powerful data processing software, Creative Biostructure supports the observation and characterization of coronavirus-like particles and/or the complex of virus-like particle (VLP) with other biomolecule using single-particle cryo-EM technology.

Application of Single Particle Cryo-EM in Virology

Cryo-EM has been utilized to study virus morphology for decades, resolving the three-dimensional (3D) structure of viruses such as Zika, Ebola, and coronavirus. Due to the tremendous progress of electronic detectors and image processing technology in recent years, cryo-EM single-particle analysis has gradually become one of the main approaches for determining the 3D structure of biological samples, especially an essential tool in the study of virus structure and dynamics. In the early stage of novel coronavirus (SARS-CoV-2) outbreak, scientists obtain significant advances in the structure and behavior of novel coronavirus using this technology, including a series of biophysical information of viral particles and the process of viral infection.

Some studies on the structure of complexes of viral particles and antibodies are essential to better understand the molecular mechanism behind antigen-antibody interactions. Moreover, cryo-EM single-particle analysis technology is increasingly used in epitope mapping to define specific binding sites. These studies accelerate the discovery and development of more specific and effective vaccines or antiviral therapeutics.

Coronavirus structure mapped with cryo-EM.  Figure 1. Coronavirus structure mapped with cryo-EM.

Our Single Particle Cryo-EM Services for Coronavirus-like Particle

For coronaviruses without strong infectivity, we can support the use of this technology to obtain the biophysical information of the virus, including its morphology and outer-shell proteins, as well as to observe the interaction mode of viral particles and receptors. Considering safety issues, we do not support the observation of native coronavirus samples that can cause large-scale human infections, such as SARS-CoV and novel coronavirus.

We can use cryo-EM single-particle analysis technology to visualize coronavirus-like particles. VLP is a multi-protein structure assembled from native viral structural proteins. It has the structure and conformation of native viruses, but does not contain any genetic material, so it is non-infectious and easy to handle. VLP is becoming an increasingly common tool for drug delivery system development, antibody screening, and vaccine development. The service allows the 3D structure reconstruction of your coronavirus-like particles to characterize these nanoscale VLPs. To expand other applications, we can also use this technology to observe the interaction between VLP and other biomolecules (such as neutralizing antibody). We can design and develop custom coronavirus-like particles and provide off-the-shelf VLP products of the family Coronaviridae.

Creative Biostructure has been optimizing our cryo-EM single-particle analysis technology. We have extensive experience in sample preparation, imaging, data collection, data processing, and structural analysis. In addition to the visualization of coronavirus-like particles, we provide specialized services for the 3D structural analysis of proteins involved in coronavirus infection. Please feel free to contact us for more details.

Contact us to discuss your project!


  1. Wrapp D.; et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020, 367(6483): 1260-1263.

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