9CPK
D8 symmetry reconstruction of MmCPn in closed state
Summary for 9CPK
| Entry DOI | 10.2210/pdb9cpk/pdb |
| EMDB information | 45793 |
| Descriptor | Chaperonin, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | archaea chaperonin in closed state with atp/alfx, chaperone |
| Biological source | Methanococcus maripaludis |
| Total number of polymer chains | 16 |
| Total formula weight | 941837.49 |
| Authors | Yanyan, Z. (deposition date: 2024-07-18, release date: 2025-07-30, Last modification date: 2025-10-08) |
| Primary citation | Zhao, Y.,Schmid, M.F.,Chiu, W. Cost-benefit analysis of cryogenic electron tomography subtomogram averaging of chaperonin MmCpn at near atomic resolution. Structure, 33:372-380.e2, 2025 Cited by PubMed Abstract: Cryogenic electron microscopy single particle analysis (cryoEM-SPA) has evolved into a routine approach for determining macromolecule structures to near-atomic resolution. Cryogenic electron tomography subtomogram averaging (cryoET-STA) toward a similar resolution, in contrast, is still under active development. Here, we use the archeal chaperonin MmCpn as a model macromolecule to quantitatively investigate the resolution limiting factors of cryoET-STA in terms of cumulative electron dose, ice thickness, subtomogram numbers, and tilt angle ranges. By delineating the feasibility and experimental factors of attaining near atomic resolution structure with cryoET-STA, especially the effect of electron damage through the tilt series and inelastic scattering at various ice thickness, we encourage a customized tilt series collection strategy for efficient throughput. This study provides a biophysical basis for the application of cryoET-STA (for highly symmetric molecules like MmCpn) toward high resolution and the rationales in using cryoET-STA to achieve an efficient outcome at the desired resolution. PubMed: 39644888DOI: 10.1016/j.str.2024.11.008 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.56 Å) |
Structure validation
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