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TitleMycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 77, Issue Pt 8, Page 1077-1083, Year 2021
Publish dateAug 1, 2021
AuthorsAbril Gijsbers / Yue Zhang / Ye Gao / Peter J Peters / Raimond B G Ravelli /
PubMed AbstractThe use of cryo-EM continues to expand worldwide and calls for good-quality standard proteins with simple protocols for their production. Here, a straightforward expression and purification protocol ...The use of cryo-EM continues to expand worldwide and calls for good-quality standard proteins with simple protocols for their production. Here, a straightforward expression and purification protocol is presented that provides an apoferritin, bacterioferritin B (BfrB), from Mycobacterium tuberculosis with high yield and purity. A 2.12 Å resolution cryo-EM structure of BfrB is reported, showing the typical cage-like oligomer constituting of 24 monomers related by 432 symmetry. However, it also contains a unique C-terminal extension (164-181), which loops into the cage region of the shell and provides extra stability to the protein. Part of this region was ambiguous in previous crystal structures but could be built within the cryo-EM map. These findings and this protocol could serve the growing cryo-EM community in characterizing and pushing the limits of their electron microscopes and workflows.
External linksActa Crystallogr D Struct Biol / PubMed:34342280 / PubMed Central
MethodsEM (single particle)
Resolution2.1 Å
Structure data

12738

7o6e

EMDB-12738, PDB-7o6e:
2.12 A cryo-EM structure of Mycobacterium tuberculosis Ferritin
Method: EM (single particle) / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsMETAL TRANSPORT / Iron storage; Ferroxidase; Bacterial Ferritin; Octahedral symmetry.

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