Cited by 1,060SARS-CoV-2 and COVID-19 ResearchAdvanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

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Molecular Architecture of the SARS-CoV-2 Virus

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Yao, Hangping, Song, Yutong, Chen, Yong, Wu, Nanping, Xu, Jialu, Sun, Chujie, Zhang, Jiaxing, Weng, Tianhao, Zhang, Zheyuan, Wu, Zhigang, Cheng, Linfang, Shi, Danrong, Lu, Xiangyun, Lei, Jianlin, Crispin, Max, Shi, Yigong, Li, Lanjuan, Li, Sai·2020·Cell

DOI 10.1016/j.cell.2020.09.018PMC PMC7474903

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Abstract

SARS-CoV-2 is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryoelectron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in pre- and postfusion conformations were determined to average resolutions of 8.7-11 Å. Compositions of the N-linked glycans from the native spikes were analyzed by mass spectrometry, which revealed overall processing states of the native glycans highly similar to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNPs) and their higher-order assemblies were revealed. Overall, these characterizations revealed the architecture of the SARS-CoV-2 virus in exceptional detail and shed light on how the virus packs its ∼30-kb-long single-segmented RNA in the ∼80-nm-diameter lumen.

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BackgroundInfluential
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Background
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Background
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BackgroundInfluential
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Result
Detecting residual chemical disinfectant using an atomic Co–N x –C anchored neuronal-like carbon catalyst modified amperometric sensor
Li, Z., Jiang, G., Wang, Y., Tan, M., Cao, Y., Tian, E., Zhang, L., Chen, X., Zhao, M., Jiang, Y., et al. (2022) · Environmental Science Nano · doi:10.1039/d1en01111a · Cited by 5
Development and Testing of a Low-Cost Inactivation Buffer That Allows for Direct SARS-CoV-2 Detection in Saliva
Bustos-García, B., Garza-Manero, S., Cano-Domínguez, N., López-Sánchez, D. M., de Oca, G. S. M., Salgado-Aguayo, A. R., Targa, F. R., Ávila‐Ríos, S., & Valdés, V. J. (2022) · Vaccines · doi:10.3390/vaccines10050730 · Cited by 5
“, spike, envelope, and membrane) [28], while inside the capsid, the viral RNA genome is assembled as ribonucleoprotein complexes [21].”
Background
Single-particle detection of native SARS-CoV-2 virions by microfluidic resistive pulse sensing
Varga, Z., Madai, M., Kemenesi, G., Beke‐Somfai, T., & Jakab, F. (2022) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2022.112716 · Cited by 5
“used cryo-EM to investigate the ultrastructure of SARS-CoV-2 virions and obtained 80 nm for the average envelope diameter and 26 ± 15 for the number of spikes (S trimers) per virion [6].”
Advances in computational approaches to structure determination of alphaviruses and flaviviruses using cryo-electron microscopy.
Lata, K., Charles, S., & Prasad, V. M. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.107993 · Cited by 4
Potential SARS-CoV-2 Nonstructural Protein 15 Inhibitors: Repurposing FDA-Approved Drugs
Tang, J. Y., Tsigelny, I. F., Greenberg, J. P., Miller, M. A., & Kouznetsova, V. L. (2021) · Journal of Exploratory Research in Pharmacology · doi:10.14218/jerp.2021.00032 · Cited by 5
Modulation of Biophysical Properties of Nucleocapsid Protein in the Mutant Spectrum of SARS-CoV-2Preprint
Nguyen, A., Zhao, H., Myagmarsuren, D., Srinivasan, S., Wu, D., Chen, J., Piszczek, G., & Schuck, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.21.568093 · Cited by 5
Integrin β3 N125 glycosylation is essential for human cytomegalovirus entry into fibroblasts
Zheng, L., Pan, T., Wang, H., He, Z., & Tian, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144322 · Cited by 4
Filtering evaluation of multiplex respiratory virus-like particles by machine learning-assisted surface-enhanced Raman spectroscopy
Song, S., Kim, S., Lee, J. S., Kang, H. W., Seok, J. H., Park, M., Choi, N., Sung, Y. J., & Sim, S. J. (2025) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2025.138152 · Cited by 4
Unveiling the silent threat: COVID-19 and myocardial injury
Xu, K., He, W., Yu, B., Wang, J. J., Wu, J., & Wang, D. W. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108904 · Cited by 4
Urea induced characterization & structural dynamics of the Nucleocapsid Protein using biophysical and in silico approaches
Samad, A., Imam, M. A., Alam, D., Ahmed, A., Islam, A., & Parveen, S. (2025) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2025.144515 · Cited by 4
TMPRSS2-mediated coronavirus spike activation and inhibition
McCallum, M., Case, J. B., Brown, J. T., Park, Y., Lee, J., Sutherland, E., Aggarwal, A., Gibson, C. A., Lempp, F. A., Stewart, C., et al. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01801-y · Cited by 5
Neurogenesis and neuroplasticity activities of natural products: therapeutic potential in Alzheimer’s disease
Shaheen, A. M., Mousa, M. H. A., Hindam, M. O., El‐Dessouki, A. M., Fahim, S. A., Hal, D. M., Ahmed, S., El‐Shiekh, R. A., & Khalifa, H. O. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1863841 · Cited by 4
“Modification can decrease the amount of BDNF available at synapses, ultimately weakening mechanisms of synaptic plasticity and neuronal adaptability (Yao et al., 2020).”
High sensitivity and enhanced measurement range biosensing based on defective photonic crystal microring resonators
Su, J.-Y., Huang, X.-Q., Xu, H.-L., Zhou, J., & Meng, Z. (2022) · Journal of the Optical Society of America B · doi:10.1364/josab.470215 · Cited by 4
An overview of SARS-CoV-2 viral proteins with relevance to improved diagnostic and therapeutic platforms
Chung, C. W., Irudayaraj, P., Lallow, E. O., Xu, Z., Park, Y. K., Kudchodkar, S. B., Montaner, L. J., Srinivasan, A., & Muthumani, K. (2024) · Frontiers in Virology · doi:10.3389/fviro.2024.1399993 · Cited by 5
G-quadruplex-forming small RNA inhibits coronavirus and influenza A virus replication
Sekine, R., Takeda, K., Suenaga, T., Tsuno, S., Kaiya, T., Kiso, M., Yamayoshi, S., Takaku, Y., Ohno, S., Yamaguchi, Y., et al. (2025) · Communications Biology · doi:10.1038/s42003-024-07351-7 · Cited by 4
“The architecture of the SARS-CoV-2 RNA – NP ultrastructure is likely based on protein – protein interaction and the interaction of the NP and vRNA 26 .”
Structural glycobiology – from enzymes to organelles
Mycroft‐West, C. J., Leanca, M. A., & Wu, L. (2025) · Biochemical Society Transactions · doi:10.1042/bst20241119 · Cited by 4
PBS-DLS: A Novel Ultrasensitive Dynamic Light Scattering Immunoassay
Fang, H., Gong, T., Su, Y., Xiong, S., Yao, M., Guo, Q., Tong, W., Gan, T., Zhang, P., Liu, Q., et al. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c03548 · Cited by 4
Cryo-EM to visualize the structural organization of viruses
de Oliveira, G. A. P., & Silva, J. L. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.04.011 · Cited by 6
Stem cell-based therapy for COVID-19
Chen, X., Liu, B., Li, C., Wang, Y., Geng, S., Du, X., Weng, J., & Lai, P. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110890 · Cited by 4
Integrated Immunopeptidomics and Proteomics Study of SARS-CoV-2–Infected Calu-3 Cells Reveals Dynamic Changes in Allele-specific HLA Abundance and Antigen Presentation
Chen, R., Fulton, K. M., Tran, A., Duque, D., Kovalchik, K. A., Caron, É., Twine, S. M., & Li, J. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100645 · Cited by 4
Inducing enhanced neutralizing antibodies against broad SARS-CoV-2 variants through glycan-shielding multiple non-neutralizing epitopes of RBD
Zhang, Q., Yang, Y., Lan, J., Wang, Z., Gao, Y., Li, X., Mao, W., Xie, J., Mi, L.-Z., Zhang, X., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1259386 · Cited by 4
“Results showed that the maximum neutralizing ability of gsRBD-immunized sera against the Omicron (BQ.1.1) pseudovirus decreased by 40%-60% compared to the Omicron (B.1.1.529) strain (Supplementary Figures 7F, 8).”
BackgroundResultInfluential
Rapid Determination of SARS-CoV-2 Integrity and Infectivity by Using Propidium Monoazide Coupled with Digital Droplet PCR
Sberna, G., Mija, C., Lalle, E., Rozera, G., Matusali, G., Carletti, F., Girardi, E., & Maggi, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116156 · Cited by 4
“…3 and 4 showed a mean viral load of 1.4 Log copies/mL via a ddPCR. SARS-CoV-2, a highly infectious virus responsible for the COVID-19 pandemic [26 underscores the need for rapid methods to assess the risk of SARS-CoV-2 infection without When treated with PMAxx, the viral load decreased by a…”
MethodInfluential
Optical detection of infectious SARS-CoV-2 virions by counting spikes
Kudryavtsev, D. S., Mozhaeva, V. A., Ivanov, I. A., Siniavin, A. E., Kalmykov, A. S., Gritchenko, A. S., Khlebtsov, B. N., Wang, S., Kang, B., Tsetlin, V. I., et al. (2024) · Nanoscale · doi:10.1039/d4nr01236d · Cited by 4
Application of advanced bioimaging technologies in viral infections
Sun, Y., Cao, C., Peng, Y., Dai, X., Li, X., Li, J., Liang, T., Song, P., Ye, Y., Yang, J., et al. (2024) · Materials Today Physics · doi:10.1016/j.mtphys.2024.101488 · Cited by 4
Current development of severe acute respiratory syndrome coronavirus 2 neutralizing antibodies (Review)
Zhang, T., Yang, D., Tang, L., & Hu, Y. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13272 · Cited by 5
Unraveling the structural and functional dimensions of SARS-CoV2 proteins in the context of COVID-19 pathogenesis and therapeutics
Jhanwar, A., Sharma, D., & Das, U. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134850 · Cited by 4
Impaired instructive and protective barrier functions of the endothelial cell glycocalyx pericellular matrix is impacted in COVID ‐19 disease
Smith, M. M., & Melrose, J. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70033 · Cited by 4
“70 The SARS- CoV-2 virion is an enveloped particle with a diameter of around 60–100 nm. 71 ACE2 is accepted as the main host cell receptor on host cells.”
Mechanisms of Plasma Ozone and UV-C Sterilization of SARS-CoV-2 Explored through Atomic Force Microscopy
Bae, J., Bednář, P., Zhu, R., Bong, C., Bak, M. S., Stainer, S., Kim, K., Lee, J.-H., Yoon, C., Lee, Y., et al. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c11057 · Cited by 4
“32 We assume that the ozone-induced damage can decrease the Young’s modulus of the outer layer, leading to swelling of the virus particles.”
Targeting viral suppressor of RNAi confers anti-coronaviral activity
Chen, J., Mu, J., Zhou, K., Zhang, Y., Zhang, J., Shu, T., Shang, W., Ren, Y., Xu, X.-Q., Zhang, L., et al. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.12.009 · Cited by 4
Self-citation
Structural biology of SARS-CoV-2 nucleocapsid
Kippes, O., Thorn, A., & Santoni, G. (2022) · Crystallography Reviews · doi:10.1080/0889311x.2022.2072835 · Cited by 4
“These may act with the RNA in a ‘beads on a string’ (see Figure 3(B)) stoichiometry [37].”
Background
Can plant-derived anti-HIV compounds be used in COVID-19 cases?
Das, D., Jena, A. B., Banerjee, A., Radhakrishnan, A., Duttaroy, A. K., & Pathak, S. (2022) · Medical Hypotheses · doi:10.1016/j.mehy.2022.110926 · Cited by 4
“Coronavirus strains A2A and A3I make up the majority of infections in Indian patients.”
Influential
Disinfection Effect of Hexadecyl Pyridinium Chloride on SARS-CoV-2 in vitro
Chen, K., Ma, F., Wang, Q.-J., Wang, Y., Zhuang, X., Zhang, X.-N., Mao, H., & Zhang, Y. (2022) · Intervirology · doi:10.1159/000526241 · Cited by 4
“Yao et al. [9] reported the first full three-dimensional fine structure of SARS-CoV-2, while Zhou et al. [7] re-ported the full-length genome of 2019-nCoV.”
Background
Coronavirus peplomer interaction
Pak, M. C., Chakraborty, R., Kanso, M. A., Tontiwattanakul, K., Kim, K.-I., & Giacomin, A. J. (2022) · Physics of Fluids · doi:10.1063/5.0120167 · Cited by 4
Structural characteristics of the SARS-CoV-2 Omicron lineages BA.1 and BA.2 virions
Ma, X., Wang, Y., Gao, Y., Wang, Y., Yan, A., Chen, J., Zhang, L., Wang, P., Zhao, J., & Liu, Z. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01385-9 · Cited by 4
“In contrast, the wild type (WT) SARSCoV-2 virions are oblate spheroidal.(1) The mean diameter of Omicron BA.”
BackgroundMethodResult
ACE2 Receptor: A Potential Pharmacological Target in COVID-19
Zhu, Y., Zhang, S., Wang, Z., Wang, Z., & Zhu, S. (2023) · Current Protein and Peptide Science · doi:10.2174/1389203724666230816092518 · Cited by 4
Condensates of SARS-CoV-2 Nucleoprotein on Viral RNA and Their Small Molecule Modulators (A Review)
Svetlova, Y. I., Pavlova, I., Aralov, A. V., & Varizhuk, A. M. (2023) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162023050229 · Cited by 4
Human ACE2 protein is a molecular switch controlling the mode of SARS-CoV-2 transmission
Yang, C. S., Liao, C., Hsu, H.-W., Liang, J., Chang, C.-S., Ko, H., Chang, R.-H., Tang, W., Chang, M.-H., Wang, I.-H., et al. (2023) · Journal of Biomedical Science · doi:10.1186/s12929-023-00980-w · Cited by 4
“4c, arrow) with a diameter of 80–100 nm, the size of which was similar to the size of SARS-CoV-2 [25, 26].”
Result
Development of Fluorescence-Based Assays for Key Viral Proteins in the SARS-CoV-2 Infection Process and Lifecycle
Deng, M., Zhang, C., Yan, W., Chen, L., He, B., & Li, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052850 · Cited by 4
“…inhibit its spread, replication, and proliferation, and to curb the continued spread of the epidemic world-wide, researchers have used sub-atomic resolution three-dimensional averaging (STA) and cryo-electron tomography (Cryo-ET) techniques to reveal the true molecular structure of SARS-CoV-2 [14].”
Background
Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments
Roy, R. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1292588 · Cited by 4
Allosteric modulation by the fatty acid site in the glycosylated SARS-CoV-2 spike
Oliveira, A. S. F., Kearns, F. L., Rosenfeld, M. A., Casalino, L., Tulli, L., Berger, I., Schaffitzel, C., Davidson, A. D., Amaro, R. E., & Mulholland, A. J. (2024) · eLife · doi:10.7554/elife.97313.3 · Cited by 7
Coronavirus disease 2019 vaccines: landscape of global studies and potential risks
Jiang, H.-D., Tao, Y., Jia, S., Li, J., & Zhu, F. (2021) · Chinese Medical Journal · doi:10.1097/cm9.0000000000001688 · Cited by 4
“Recent studies have shown that the heptad repeat 2 (HR2) in the S2 subunit may trigger a metastable state of the S protein and promote conformational changes, thereby achieving immune escape.([33]) Animal experiments have also confirmed that an HR2deficient SARS-CoV-2 S protein can induce higher neutralizing antibody…”
Background
IsoExplorer: an isosurface-driven framework for 3D shape analysis of biomedical volume data
Dai, H., Tao, Y., He, X., & Lin, H. B. (2021) · Journal of Visualization · doi:10.1007/s12650-021-00770-2 · Cited by 4
“…5159 H-CoV Spike (Park et al. 2019) 280 (cid:4) 280 (cid:4) 280 3149 PD-CoV Spike (Shang et al. 2018) 256 (cid:4) 256 (cid:4) 256 2868 SARS-CoV-2 (Yao et al. 2020) 512 (cid:4) 512 (cid:4) 512 3071 SARS-CoV-2 Spike up (Melero et al. 2020) 432 (cid:4) 432 (cid:4) 432 10 SARS-CoV-2 Spike down 1…”
BackgroundInfluential
Nanomaterials and Biosensing Technology for the SARS-CoV-2 Detection
Yanyan, L. I., Peng, Y., Lin, C., Luo, X., Teng, Z., ZHANG, X., HUANG, Z., & Yang, Y. (2022) · Journal of Inorganic Materials · doi:10.15541/jim20220218 · Cited by 4
Mechanics of diffusion-mediated budding and implications for virus replication and infection
Bacca, M. (2022) · Journal of The Royal Society Interface · doi:10.1098/rsif.2022.0525 · Cited by 4
“The input energy is extracted from Figure 3b, and the predictions are compared against the observed median virion sizes for SARS-CoV-1 & 2 [7-9], HIV-1 [10], Flu [11-12], and HCV (Hepatitis C) [13-14].”
BackgroundMethodInfluential
The “LLQY” Motif on SARS-CoV-2 Spike Protein Affects S Incorporation into Virus Particles
Du, S., Xu, W., Wang, Y., Li, L., Hao, P., Tian, M., Wang, M., Li, T., Wu, S.-P., Liu, Q., et al. (2022) · Journal of Virology · doi:10.1128/jvi.01897-21 · Cited by 5
“domains with three flexible hinges in the S2 subunit (4, 20).”
BackgroundSelf-citation
A Facile Single-Phase-Fluid-Driven Bubble Microfluidic Generator for Potential Detection of Viruses Suspended in Air
Man, J., Man, L., Zhou, C., Li, J., Liang, S., Zhang, S., & Li, J. (2022) · Biosensors · doi:10.3390/bios12050294 · Cited by 4
“To simulate the size of the COVID-19 virus [35], 100 nm sized fluorescent Nile Red nanoparticles were used to simulate the virus within the exhaled droplets since it was difficult to receive the required qualifications to perform virus-spread experiments.”
Method
Morphological Features and Divergence of SARS-CoV 2 and SARS-CoV Virus Using TEM ImagesPreprint
Taha, B. A., Mashhadany, Y. I. M. A., Al-Jubouri, Q., Zan, M. S. D., Luo, Y., Li, M., & Arsad, N. (2022) · Research Square · doi:10.21203/rs.3.rs-1336182/v1 · Cited by 4
Toward Atomistic Models of Intact SARS-CoV-2 via Martini Coarse-Grained Molecular Dynamics SimulationsPreprint
Wang, D., Li, J., Wang, L., Cao, Y., Li, S., & Song, C. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.31.478415 · Cited by 4
“Thus, the RNP unit structure was obtained by aligning five N protein dimers into the density map (EMD-30429) (Fig.”
BackgroundMethodResultInfluentialSelf-citation
Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acidPreprint
Zhao, H., Syed, A. M., Khalid, M. M., Nguyen, A., Ciling, A., Wu, D., Yau, W., Srinivasan, S., Esposito, D., Doudna, J. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.22.568361 · Cited by 4
Electron microscopy images and morphometric data of SARS-CoV-2 variants in ultrathin plastic sections
Hoffmann, T., Michel, J., Nitsche, A., Mache, C., Schulze, J., Wolff, T., & Laue, M. M. (2024) · Scientific Data · doi:10.1038/s41597-024-04182-3 · Cited by 4
Resurrection of the Helical Hairpin Hypothesis for Understanding Coronavirus Fusion
Lall, S., Vijayasarathy, M., Joshi, N. V., & Balaram, P. N. (2025) · The Journal of Membrane Biology · doi:10.1007/s00232-025-00350-7 · Cited by 3
“1A) (Ke et al. 2020; Turonova et al. 2020; Yao et al. 2020).”

Authors: Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., Cheng, L., Shi, D., Lu, X., Lei, J., Crispin, M., Shi, Y., Li, L., & Li, S.
Affiliations: First Affiliated Hospital Zhejiang University (CN)
Tsinghua University (CN)
Center for Life Sciences (CN)
University of Southampton (GB)
Westlake University (CN)
Corresponding author: Li, Lanjuan
Li, Sai
ORCID: Yao, Hangping
Song, Yutong
Chen, Yong
Wu, Nanping
Xu, Jialu
Zhang, Jiaxing
Zhang, Zheyuan
Wu, Zhigang
Lu, Xiangyun
Lei, Jianlin
Crispin, Max
Shi, Yigong
Li, Lanjuan
Li, Sai
Venue: Cell
Publisher: Elsevier BV
Published: 2020-10
Volume: 183
Issue: 3
Pages: 730-738.e13
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2020.09.018
PMC: PMC7474903
OpenAlex: W3083130172
Cited by: 1,060
References: 82
Citations by year: 2026: 78 · 2025: 98 · 2024: 157 · 2023: 201 · 2022: 236 · 2021: 252 · 2020: 38
FWCI: 23.88
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 393 d)
Locations: Cell (publishedVersion)
bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
SSRN Electronic Journal (acceptedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (acceptedVersion)
Funders: Zhejiang University
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: SARS-CoV-2, spike protein, N-glycans, ribonucleoprotein, viral RNA packaging, viral assembly
MeSH terms: Betacoronavirus, SARS-CoV-2, Animals, Chlorocebus aethiops, Humans, Models, Molecular, Protein Conformation, Mass Spectrometry, Vero Cells, Viral Proteins, Virus Cultivation, Virus Assembly, Cryoelectron Microscopy

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