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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Self-citation
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
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BackgroundInfluential
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Background
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Background
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BackgroundSelf-citation
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Background
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Advanced descriptors for long-range noncovalent interactions between SARS-CoV-2 spikes and polymer surfaces
Luca, G. D., Petrosino, F., Salvo, J. L. D., Chakraborty, S., & Curcio, S. (2021) · Separation and Purification Technology · doi:10.1016/j.seppur.2021.120125 · Cited by 8
“Considering certain flexibility of the bi-lipidic membrane due to the pleomorphism of the virion [41,42], the global potentials were evaluated (Fig.”
Sensitivity of SARS-CoV-2 Life Cycle to IFN Effects and ACE2 Binding Unveiled with a Stochastic Model
SAZONOV, I. A., Grebennikov, D. S., Meyerhans, A., & Bocharov, G. A. (2022) · Viruses · doi:10.3390/v14020403 · Cited by 8
“To this end, the model parameter representing the rate constant of virion binding to the ACE2 receptor kbind is varied from its basal value by 10 times to cover the range of observed increase or decrease in the binding affinities [14,53].”
Background
Human genetic factors associated with pneumonia risk, a cue for COVID-19 susceptibility
Guin, D., Yadav, S., Singh, P., Singh, P., Thakran, S., Kukal, S., Kanojia, N., Paul, P. R., PATTNAIK, B. R., Sardana, V., et al. (2022) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2022.105299 · Cited by 8
Evolutionary Pattern Comparisons of the SARS-CoV-2 Delta Variant in Countries/Regions with High and Low Vaccine Coverage
Zhang, J., Fan, L.-Q., Xu, H., Fu, Y.-H., Peng, X.-L., Zheng, Y.-P., Yu, J., & He, J. (2022) · Viruses · doi:10.3390/v14102296 · Cited by 9
“SARS-CoV-2 is a virus with large genome, about 30 kb in length, and has been reported to accumulate two mutations per month in the global population [8,9].”
BackgroundSelf-citation
Connecting Single Nucleotide Polymorphisms, Glycosylation Status and Interactions of Acute-Phase Plasma Proteins
Wu, D., Guo, M., & Robinson, C. V. (2022) · Chem · doi:10.1016/j.chempr.2022.11.018 · Cited by 8
Advanced Vaccine Design Strategies against SARS-CoV-2 and Emerging Variants
Zhang, J., Xia, Y., Liu, X., & Liu, G. (2023) · Bioengineering · doi:10.3390/bioengineering10020148 · Cited by 8
“Among the encoded structural proteins (membrane (M) protein, nucleocapsid (N) protein, Envelope (E) protein, and spike (S) protein) [48,49], the envelope glycoprotein spike (S) confers SARS-CoV-2 crown-like appearance (corona) [50,51] (Figure 1B,C), and more critically, the spike is a protein that binds to the angiote…”
BackgroundSelf-citation
Inactivation and spike protein denaturation of novel coronavirus variants by CuxO/TiO2 nano-photocatalysts
Tatsuma, T., Nakakido, M., Ichinohe, T., Kuroiwa, Y., Tomioka, K., Liu, C., Miyamae, N., Onuki, T., Tsumoto, K., Hashimoto, K., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-30690-0 · Cited by 8
COVID-19 Diagnosis and SARS-CoV-2 Strain Identification by a Rapid, Multiplexed, Point-of-Care Antibody Microarray
Heggestad, J. T., Britton, R. J., Kinnamon, D., Liu, J., Anderson, J. G., Joh, D. Y., Quinn, Z., Fontes, C. M., Hucknall, A., Parks, R., et al. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.2c05180 · Cited by 8
The Effect of Select SARS-CoV-2 N-Linked Glycan and Variant of Concern Spike Protein Mutations on C-Type Lectin-Receptor-Mediated Infection
Bains, A., Guan, W., & LiWang, P. J. (2023) · Viruses · doi:10.3390/v15091901 · Cited by 9
Nucleocapsid proteins from human coronaviruses possess phase separation capabilities and promote FUS pathological aggregation
Dong, H., Zhang, H., Jalin, J., He, Z., Wang, R., Huang, L., Liu, Z., Zhang, S., Dai, B., & Li, D. (2023) · Protein Science · doi:10.1002/pro.4826 · Cited by 8
“…indicates that LLPS of the N protein from SARS-CoV-2 is involved in forming condensed protein-nucleic acid compartments and packaging its genome into new virions, a crucial step in the virus' life cycle (Lu et al., 2021; Cubuk et al., 2021; Yao et al., 2020; Nikola-kaki and Giannakouros, 2020).”
Background
Membrane Condensation and Curvature Induced by SARS-CoV-2 Envelope Protein
Wölk, C., Shen, C. C., Hause, G., Surya, W., Torres, J., Harvey, R. D., & Bello, G. (2024) · Langmuir · doi:10.1021/acs.langmuir.3c03079 · Cited by 8
“44 The mostly fluid phase membranes of the ERGIC might be susceptible to E protein regardless of the PS content and in a way that favors the curvature and budding processes during viral replication.”
Combinatorial Approach with Mass Spectrometry and Lectin Microarray Dissected Site-Specific Glycostem and Glycoleaf Features of the Virion-Derived Spike Protein of Ancestral and γ Variant SARS-CoV-2 Strains
Hiono, T., Sakaue, H., Tomioka, A., Kaji, H., Sasaki, M., Orba, Y., Sawa, H., & Kuno, A. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00874 · Cited by 8
Nano-targeting lessons from the SARS-CoV-2
Ribeiro, I. R. S., da Silva, R. F., Silveira, C. P., Galdino, F. E., & Cardoso, M. B. (2020) · Nano Today · doi:10.1016/j.nantod.2020.101012 · Cited by 8
Vesicle Formation by the Self-Assembly of Gold Nanoparticles Covered with Fluorinated Oligo(ethylene glycol)-Terminated Ligands and Its Stability in Aqueous Solution
Wei, J., Huang, X., Zhang, L., Chen, Y., Niikura, K., Mitomo, H., Ijiro, K., & Zhang, Z. (2021) · Langmuir · doi:10.1021/acs.langmuir.1c00996 · Cited by 8
Self-citation
Impact of the COVID-19-induced lockdown on the incidence of ocular trauma presenting to a tertiary care hospital
Pande, R., Mohod, S., Padmapriya, V., Shanbhag, S., & Nandish, S. (2022) · BMJ Open Ophthalmology · doi:10.1136/bmjophth-2021-000861 · Cited by 8
Up, up, down, down: the structural biology of the SARS-CoV-2 spike protein and how it cheats the immune system
Stäb, S., Pearce, N. M., Tronrud, D. E., Ginn, H. M., Fadda, E., Santoni, G., & Thorn, A. (2024) · Crystallography Reviews · doi:10.1080/0889311x.2024.2363756 · Cited by 7
“The sparse distribution of spikes on the viral envelope of SARS-CoV-2 particles may be crucial for allowing this flexibility, a characteristic that is markedly distinct to other class I fusion proteins [179,181].”
Influential
A comprehensive review of current insights into the virulence factors of SARS-CoV-2
Wang, Y., Xia, B., & Gao, Z. (2025) · Journal of Virology · doi:10.1128/jvi.02049-24 · Cited by 7
“The S2 subunit plays a critical role in facilitating the fusion of the viral and host cell membranes and contains the fusion peptide, two heptad repeats (HR1 and HR2), the transmembrane domain, and the cytoplasmic tail (67, 68).”
COVID-19 and diabetes mellitus: a review of the incidence, pathophysiology and management of diabetes during the pandemic
Faruqi, J., & Balasubramanyam, A. (2023) · Expert Review of Endocrinology & Metabolism · doi:10.1080/17446651.2023.2176300 · Cited by 10
SARS-CoV-2 S Glycoprotein Stabilization Strategies
Pedenko, B., Sulbarán, G., Guilligay, D., Effantin, G., & Weissenhorn, W. (2023) · Viruses · doi:10.3390/v15020558 · Cited by 8
The Impact of COVID-19 on People Living with HIV-1 and HIV-1-Associated Neurological Complications
Dutta, D., Liu, J., & Xiong, H. (2023) · Viruses · doi:10.3390/v15051117 · Cited by 7
SARS-CoV-2 virus-like-particles via liposomal reconstitution of spike glycoproteins
McColman, S., Shkalla, K., Sidhu, P., Liang, J., Osman, S., Kovacs, N., Bokhari, Z., Marques, A. C. F., Li, Y., Lin, Q., et al. (2023) · Nanoscale Advances · doi:10.1039/d3na00190c · Cited by 7
In Situ Single Particle Reconstruction Reveals 3D Evolution of PtNi Nanocatalysts During Heating
Wang, Y., Slater, T. J. A., Leteba, G. M., Lang, C. I., Wang, Z. L., & Haigh, S. J. (2023) · Small · doi:10.1002/smll.202302426 · Cited by 7
Sulfated liposome-based artificial cell membrane glycocalyx nanodecoys for coronavirus inactivation by membrane fusion
Li, X., Cheng, N., Shi, D., Li, Y., Li, C., Zhu, M., Jin, Q., Wu, Z., Zhu, L., He, Y., et al. (2023) · Bioactive Materials · doi:10.1016/j.bioactmat.2023.10.021 · Cited by 7
“This membrane fusion would lead to the spike protein change from prefusion conformation to postfusion conformation, which made the spike protein showed a niddle-liked shape and let the virus lose infectivity [47,48].”
BackgroundSelf-citation
Influence of Mutations and N-Glycosylation Sites in the Receptor-Binding Domain (RBD) and the Membrane Protein of SARS-CoV-2 Variants of Concern on Antibody Binding in ELISA
Schwarze, M., Volke, D., Echeverri, J. C. R., Schick, R., Lakowa, N., Grünewald, T., Wolf, J., Borte, S., Scholz, M. R., Krizsan, A., et al. (2024) · Biology · doi:10.3390/biology13040207 · Cited by 8
“…Asn343 were confirmed by tandem mass spectrometry for the recombinant wildtype RBD expressed in HEK293S GNTI − cells (Figure 2A,B), in full agreement with previous reports [4,16,38–40], and the alpha, beta, gamma, and kappa RBDs expressed in HEK293S GnTI − cells (Supplement, Figure S2) [12,18,19].”
Result
Structural stabilization of the intrinsically disordered SARS-CoV-2 N by binding to RNA sequences engineered from the viral genome fragment
Landeras-Bueno, S., Hariharan, C., Díaz-Avalos, R., Norris, A. S., Snyder, D. T., Hastie, K. M., Harkins, S., Zandonatti, M. A., Rajamanickam, R. R., Olmedillas, E., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61861-4 · Cited by 7
“1D, E) whose volume and diameter (~15nm) resemble the nucleosome-like structures or vRNPs found in intact virions by in situ tomography 29 (Supplementary Fig.”
Three-dimensional insights into human enveloped viruses in vitro and in situ
Vankadari, N., Shepherd, D. C., Carter, S. D., & Ghosal, D. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210433 · Cited by 7
Neutralization Heterogeneity of Circulating SARS-CoV-2 Variants to Sera Elicited by a Vaccinee or Convalescent
Zhang, M., Gong, Y., & Jiao, S. (2022) · Future Virology · doi:10.2217/fvl-2021-0100 · Cited by 7
“SARS-CoV-2 encodes at least 29 proteins in its (+) RNA genome, among the four structure proteins (the spike [S], membrane [M], envelope [E] and nucleocapsid [N] proteins), with S and N proteins representing the most distinctive features of the virus [13,14].”
Background
Constructing high-accuracy theoretical Raman spectra of SARS-CoV-2 spike proteins based on a large fragment method
Ni, S., Yang, Q., Huang, J., Zhou, M., Wei, L. C., Yang, Y., Wen, J., Mo, W., Le, W., Qi, D., et al. (2022) · Chemical Physics Letters · doi:10.1016/j.cplett.2022.139663 · Cited by 7
Finite element modeling of α-helices and tropocollagen molecules referring to spike of SARS-CoV-2
Wierzbicki, T., & Bai, Y. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.05.021 · Cited by 7
“Because of the large degree of ﬂexibility, the spike’s job of searching and attaching to the host cells can be performed more easily (6–10).”
Shedding Lights on the Extracellular Vesicles as Functional Mediator and Therapeutic Decoy for COVID-19
Thakur, A. (2023) · Life · doi:10.3390/life13030840 · Cited by 7
Identifying diseases associated with Post-COVID syndrome through an integrated network biology approach
Krishna, N., Sijina, K. P., & Rajanikant, G. K. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2195003 · Cited by 9
“…may be more susceptible to COVID-19 transmission due to several factors, including intellectual disability, comprehension of the risks, and barriers to implementing proper infection control, such as communal living (Larkin & Hutton, 2017; Maguire et al., 2019; Yao, Chen, et al., 2020).”
Background
Physical virology: how physics is enabling a better understanding of recent viral invaders
Cardoso-Lima, R., Santos‐Oliveira, R., Souza, P. F. N., Barbosa, L. R. S., Wuite, G. J. L., & Alencar, L. M. R. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01075-4 · Cited by 7
Profile of SARS-CoV-2
Heinz, F. X., & Stiasny, K. (2020) · Wiener klinische Wochenschrift · doi:10.1007/s00508-020-01763-1 · Cited by 8
“The SARS-CoV-2 virus particle has the typical coronavirus morphology, with a diameter of ~80–120nm [17].”
Background
Identification, mapping and relative quantitation of SARS-CoV-2 Spike glycopeptides by Mass-Retention Time Fingerprinting
Chalk, R., Greenland, W. E. P., Moreira, T., Coker, J. A., Mukhopadhyay, S. M. M., Williams, E., Manning, C., Bohstedt, T., McCrorie, R., Fernandez‐Cid, A., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02455-w · Cited by 7
In silico studies on milk derived peptides as potential inhibitors against SARS CoV-2 spike protein receptor binding domainPreprint
Mukhopadhyay, S., & Sarkar, A. (2021) · Research Square · doi:10.21203/rs.3.rs-618799/v1 · Cited by 7
Ultrapotent SARS coronavirus-neutralizing single-domain antibodies that bind a conserved membrane proximal epitope of the spikePreprint
Cae, S. D., Molle, I. V., van Schie, L., Shoemaker, S. R., Deckers, J., Debeuf, N., Lameire, S., Nerinckx, W., Roose, K., Fijałkowska, D., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.10.531533 · Cited by 7
Biosafety level‐3 cryo‐electron tomography of active severe acute respiratory syndrome coronavirus 2 virions
Fukuhara, H., Dokainish, H. M., Kita, S., Tabata, K., Takasu, A., Huiskonen, J. T., Anraku, Y., Nomai, T., Someya, T., Senda, T., et al. (2026) · Protein Science · doi:10.1101/2023.10.10.561643 · Cited by 8
A specific phosphorylation-dependent conformational switch of SARS-CoV-2 nucleoprotein inhibits RNA bindingPreprint
Botova, M., Camacho‐Zarco, A. R., Tognetti, J., Bessa, L. M., Guseva, S., Mikkola, E. A., Salvi, N., Maurin, D., Herrmann, T., & Blackledge, M. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.22.579423 · Cited by 7
“Such structural elements have been previously identified as substructures of the viral nucleocapsid ( 15 , 16 ).”
BackgroundMethod
Human E3 ubiquitin ligases: accelerators and brakes for SARS-CoV-2 infection
Pellman, J., Goldstein, A., & Slabicki, M. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230324 · Cited by 6
Phosphorylation Changes SARS ‐ CoV ‐2 Nucleocapsid Protein's Structural Dynamics and Its Interaction With RNA
Loonen, S., van Steenis, L., Bauer, M., & Šoštarić, N. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26842 · Cited by 6
“Inside the virion, the nucleocapsid protein (N-protein) and the gRNA form ribonucleoprotein complexes (RNPs), which organize into an ordered crystalline-like “eggs- in- a-nest” shaped assembly [5, 7].”
VOICE: Visual Oracle for Interaction, Conversation, and Explanation
Jia, D., Irger, A., Besançon, L., Strnad, O., Luo, D., Björklund, J., Kouyoumdjian, A., Ynnerman, A., & Viola, I. (2025) · IEEE Transactions on Visualization and Computer Graphics · doi:10.1109/tvcg.2025.3579956 · Cited by 6
“This collaborator establishes the node hierarchies and descriptions based on a comprehensive biology literature review [26], [27].”
Chaperone Activity of SARS-CoV-2 Nucleocapsid Protein: RNA Annealing and Destabilization Mechanisms
Zargarian, L., Ai, X., Song, Z.-Y., Perez-Gorgol, L., Couprie-Diaz, E., Fossé, P., Xi, X., & Mauffret, O. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169312 · Cited by 6
Definition of the components required for selective packaging of coronavirus genomic RNA
Pata, J. D., Stevens, T. K., Kuo, L., & Masters, P. S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2513552122 · Cited by 6
“Recent cryoelectron tomographic imaging of SARS - CoV - 2 virions has overturned the long - held notion that coronavirus nucleocapsids have helical symmetry analogous to that of most negative - strand RNA viral nucleocapsids ( 17 , 18 ).”
Coronavirus genome packaging and nucleocapsid assembly
Masters, P. S. (2026) · Journal of Virology · doi:10.1128/jvi.01330-25 · Cited by 8
“5B) (80, 81).”
SARS-CoV-2 Virus-like Particles (VLPs) Specifically Detect Humoral Immune Reactions in an ELISA-Based Platform
Hirschberg, S., Bauer, H., Kamhieh‐Milz, J., Ringel, F., Harms, C., Eddin, O. K., Prüß, A., Hanack, K., & Schulze‐Forster, K. (2022) · Antibodies · doi:10.3390/antib11040076 · Cited by 6
“The viral vesicular structure is formed by the membrane (M) and the envelope (E) proteins [5,6].”
Background
Decoy peptides effectively inhibit the binding of SARS-CoV-2 to ACE2 on oral epithelial cells
Loi, L., Yang, C., Lin, Y., Su, Y.-F., Juan, Y., Chen, Y.-H., & Chang, H. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e22614 · Cited by 6
Self-citation
A Virus-Inspired Inhalable Liponanogel Induces Potent Antitumor Immunity and Regression in Metastatic Lung Tumors
Li, J., Luo, L., He, J., Yu, J., Li, X., Shen, X., Zhang, J., Li, S., Karp, J. M., & Kuai, R. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-3414 · Cited by 6
“This motivates us to mimic the viral systems to design a safe and efficient nonviral delivery system that complements the feature of LNP. Notably, SARS-CoV-2 utilizes ribonucleoproteins to efficiently tune the loading and delivery of viral RNA (27).”
BackgroundSelf-citation
Structure Transformation of Methylammonium Polyoxomolybdates via In-Solution Acidification and Solid-State Heating from Methylammonium Monomolybdate and Application as Negative Staining Reagents for Coronavirus Observation
Sukmana, N. C., Sugiarto, S., Shinogi, J., Minato, T., Kojima, T., Fujibayashi, M., Nishihara, S., Inoue, K., Cao, Y., Zhu, T., et al. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c00543 · Cited by 6
CD81 fusion alters SARS-CoV-2 Spike trafficking
Cone, A. S., Zhou, Y., McNamara, R. P., Eason, A. B., Arias, G. F., Landis, J. T., Shifflett, K., Chambers, M. G., Yuan, R., Willcox, S., et al. (2024) · mBio · doi:10.1128/mbio.01922-24 · Cited by 6
“The intact virus particle contains between 20 and 40 homotrimers on the surface, resulting in a crownlike structure when viewed by electron microscopy (EM) (21, 22).”
Background
Discovery of broad-spectrum high-affinity peptide ligands of spike protein for the vaccine purification of SARS-CoV-2 and Omicron variants
Ma, J., Huang, Y., Jia, G., Dong, X., Shi, Q., & Sun, Y. P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137059 · Cited by 6
Tetrahedral DNA Framework‐Based Spherical Nucleic Acids for Efficient siRNA Delivery
Li, J., Mao, X., Zhao, T., Fang, W., Jin, Y., Liu, M., Fan, C., & Tian, Y. (2024) · Angewandte Chemie · doi:10.1002/ange.202416988 · Cited by 6

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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