ArticleActa crystallographica. Section D, Structural biology2021
Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.
Article in Acta crystallographica. Section D, Structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Isotope Decluttering Reduces Spectral Complexity while Maintaining Protein Structure.Analytical chemistry · 2026Article
- In situ and in vitro cryo-EM reveal structures of mycobacterial encapsulin assembly intermediates.Communications biology · 2025Article
- Multi-species cryoEM calibration and workflow verification standard.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Multi-species cryoEM calibration and workflow verification standard.bioRxiv : the preprint server for biology · 2024Article
- Iron Homeostasis inBiology · 2023Review
- Article
- Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.Acta crystallographica. Section D, Structural biology · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Registered trials
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