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TitleSymmetry-adjusted cryo-EM analysis unveils the detailed linker protein CsoS2 interactions within the α-carboxysome shell.
Journal, issue, pagesPlant Physiol, Vol. 198, Issue 1, Year 2025
Publish dateApr 30, 2025
AuthorsJianxun Li / Tianpei Li / Saimeng Wang / Yu-Zhong Zhang / Lu-Ning Liu / Peng Wang /
PubMed AbstractExcessive symmetry in cryo-EM data processing can distort key structural details of bacterial microcompartments, highlighting the importance of balanced symmetry for accurate structural insights.
External linksPlant Physiol / PubMed:40341945 / PubMed Central
MethodsEM (single particle)
Resolution2.77 - 3.71 Å
Structure data

62529

9ly9

EMDB-62529: Cryo-EM map of carboxysomal midi-shell: T = 16 shell under C1 symmetry
PDB-9ly9: Cryo-EM structure of carboxysomal mid-shell: T = 16 shell under C1 symmetry.
Method: EM (single particle) / Resolution: 3.71 Å

62530

9ly8

EMDB-62530: Cryo-EM map of carboxysomal midi-shell: T = 9 shell under C1 symmetry
PDB-9ly8: Cryo-EM structure of carboxysomal midi-shell: T=9 shell under C1 symmetry
Method: EM (single particle) / Resolution: 2.77 Å

Source
  • Halothiobacillus neapolitanus (bacteria)
  • halothiobacillus neapolitanus c2 (bacteria)
KeywordsSTRUCTURAL PROTEIN / Carboxysome / shell / Icosahedron

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