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| Title | Stabilization of Ribosomal RNA of the Small Subunit by Spermidine in . |
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| Journal, issue, pages | Front Mol Biosci, Vol. 8, Page 738752, Year 2021 |
| Publish date | Nov 18, 2021 |
 Authors | Margarita Belinite / Iskander Khusainov / Heddy Soufari / Stefano Marzi / Pascale Romby / Marat Yusupov / Yaser Hashem /   |
| PubMed Abstract | Cryo-electron microscopy is now used as a method of choice in structural biology for studying protein synthesis, a process mediated by the ribosome machinery. In order to achieve high-resolution ...Cryo-electron microscopy is now used as a method of choice in structural biology for studying protein synthesis, a process mediated by the ribosome machinery. In order to achieve high-resolution structures using this approach, one needs to obtain homogeneous and stable samples, which requires optimization of ribosome purification in a species-dependent manner. This is especially critical for the bacterial small ribosomal subunit that tends to be unstable in the absence of ligands. Here, we report a protocol for purification of stable 30 S from the Gram-positive bacterium and its cryo-EM structures: in presence of spermidine at a resolution ranging between 3.4 and 3.6 Å and in its absence at 5.3 Å. Using biochemical characterization and cryo-EM, we demonstrate the importance of spermidine for stabilization of the 30 S preserving favorable conformation of the helix 44. |
 External links | Front Mol Biosci / PubMed:34869582 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.2 - 13.76 Å |
| Structure data |  EMDB-12090:  EMDB-12091: EMDB-12178, PDB-7bgd: EMDB-12179, PDB-7bge: EMDB-23052, PDB-7kwg: |
| Source |
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 Keywords | RIBOSOME / Pathogen / small ribosomal subunit / spermidine |
staphylococcus aureus subsp. aureus nctc 8325 (bacteria)
staphylococcus aureus (bacteria)