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Utilizing extensive datasets and advanced cryo\u2013electron microscopy analysis, we present structural insights into HBsAg at a near-atomic resolution of 3.7 angstroms. HBsAg homodimers assemble into subviral particles with\n            <jats:bold>\n              <jats:italic>D<\/jats:italic>\n            <\/jats:bold>\n            <jats:sub>2<\/jats:sub>\n            - and\n            <jats:bold>\n              <jats:italic>D<\/jats:italic>\n            <\/jats:bold>\n            <jats:sub>4<\/jats:sub>\n            -like quasisymmetry, elucidating the dense-packing rules and structural adaptability of HBsAg. These findings provide insights into how HBsAg assembles into higher-order filaments and interacts with the capsid to form virions.\n          <\/jats:p>","DOI":"10.1126\/science.adp1453","type":"journal-article","created":{"date-parts":[[2024,9,12]],"date-time":"2024-09-12T18:00:07Z","timestamp":1726164007000},"page":"1217-1224","update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":40,"title":["Inherent symmetry and flexibility in hepatitis B virus subviral particles"],"prefix":"10.1126","volume":"385","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5148-5210","authenticated-orcid":true,"given":"Quan","family":"Wang","sequence":"first","affiliation":[{"name":"Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, China."},{"name":"Shanghai Clinical Research and Trial Center, Shanghai, China."},{"name":"National Facility for Protein Science, Shanghai 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