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The \u03b1-CBs are of particular interest due to their small size and relative simplicity, making them ideal targets for bioengineering applications. These CBs were the first BMC observed and have been a long-studied model; however, they are challenging to study in native systems and in purified samples. Recent advances in cryogenic electron microscopy and cryogenic electron tomography have resulted in many new published structures of the shell proteins, shell assemblies, and cargo organization within the CB. These new insights have advanced the field\u2019s understanding of important structural interfaces, shed insights into once unknown domain functions, and the complex mechanisms involved in assembly and maintenance of the CB. This review highlights recently published structures of \u03b1-CB proteins and the functional and mechanistic findings of these studies.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/jb.00366-25","type":"journal-article","created":{"date-parts":[[2026,1,12]],"date-time":"2026-01-12T14:33:26Z","timestamp":1768228406000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":3,"title":["Recent insights into \u03b1-carboxysome structure, mechanism, and assembly"],"prefix":"10.1128","volume":"208","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-5288-281X","authenticated-orcid":true,"given":"Samuel L.","family":"Hartzler","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Purdue University","place":["West Lafayette, 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