7KA3
Aldolase, rabbit muscle (beam-tilt refinement x3)
Summary for 7KA3
| Entry DOI | 10.2210/pdb7ka3/pdb |
| EMDB information | 22757 |
| Descriptor | Fructose-bisphosphate aldolase A (1 entity in total) |
| Functional Keywords | glycolysis, gluconeogenesis, carbohydrate degradation, homotetramer, lyase |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 4 |
| Total formula weight | 157054.69 |
| Authors | Kearns, S.K.,Cash, J.N.,Cianfrocco, M.A.,Li, Y. (deposition date: 2020-09-29, release date: 2020-12-02, Last modification date: 2024-03-06) |
| Primary citation | Cash, J.N.,Kearns, S.,Li, Y.,Cianfrocco, M.A. High-resolution cryo-EM using beam-image shift at 200 keV. Iucrj, 7:1179-1187, 2020 Cited by PubMed Abstract: Recent advances in single-particle cryo-electron microscopy (cryo-EM) data collection utilize beam-image shift to improve throughput. Despite implementation on 300 keV cryo-EM instruments, it remains unknown how well beam-image-shift data collection affects data quality on 200 keV instruments and the extent to which aberrations can be computationally corrected. To test this, a cryo-EM data set for aldolase was collected at 200 keV using beam-image shift and analyzed. This analysis shows that the instrument beam tilt and particle motion initially limited the resolution to 4.9 Å. After particle polishing and iterative rounds of aberration correction in , a 2.8 Å resolution structure could be obtained. This analysis demonstrates that software correction of microscope aberrations can provide a significant improvement in resolution at 200 keV. PubMed: 33209328DOI: 10.1107/S2052252520013482 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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