8EMQ
Mouse apoferritin heavy chain with zinc determined using single-particle cryo-EM with Apollo camera.
Summary for 8EMQ
| Entry DOI | 10.2210/pdb8emq/pdb |
| EMDB information | 28259 |
| Descriptor | Ferritin heavy chain, N-terminally processed, ZINC ION, FE (III) ION, ... (4 entities in total) |
| Functional Keywords | bind with iron, metal binding protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 24 |
| Total formula weight | 483815.14 |
| Authors | Peng, R.,Fu, X.,Mendez, J.H.,Randolph, P.H.,Bammes, B.,Stagg, S.M. (deposition date: 2022-09-28, release date: 2022-12-21, Last modification date: 2024-06-19) |
| Primary citation | Peng, R.,Fu, X.,Mendez, J.H.,Randolph, P.S.,Bammes, B.E.,Stagg, S.M. Characterizing the resolution and throughput of the Apollo direct electron detector. J Struct Biol X, 7:100080-100080, 2023 Cited by PubMed Abstract: Advances in electron detection have been essential to the success of high-resolution cryo-EM structure determination. A new generation of direct electron detector called the Apollo, has been developed by Direct Electron. The Apollo uses a novel event-based MAPS detector custom designed for ultra-fast electron counting. We have evaluated this new camera, finding that it delivers high detective quantum efficiency (DQE) and low coincidence loss, enabling high-quality electron counting data acquisition at up to nearly 80 input electrons per pixel per second. We further characterized the performance of Apollo for single particle cryo-EM on real biological samples. Using mouse apoferritin, Apollo yielded better than 1.9 Å resolution reconstructions at all three tested dose rates from a half-day data collection session each. With longer collection time and improved specimen preparation, mouse apoferritin was reconstructed to 1.66 Å resolution. Applied to a more challenging small protein aldolase, we obtained a 2.24 Å resolution reconstruction. The high quality of the map indicates that the Apollo has sufficiently high DQE to reconstruct smaller proteins and complexes with high-fidelity. Our results demonstrate that the Apollo camera performs well across a broad range of dose rates and is capable of capturing high quality data that produce high-resolution reconstructions for large and small single particle samples. PubMed: 36578473DOI: 10.1016/j.yjsbx.2022.100080 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.66 Å) |
Structure validation
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