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8EHG

Rabbit muscle aldolase determined using single-particle cryo-EM with Apollo camera.

Summary for 8EHG
Entry DOI10.2210/pdb8ehg/pdb
EMDB information28147
DescriptorFructose-bisphosphate aldolase A (1 entity in total)
Functional Keywordsglycolysis, sugar binding protein
Biological sourceOryctolagus cuniculus (rabbit)
Total number of polymer chains4
Total formula weight157579.50
Authors
Peng, R.,Fu, X.,Mendez, J.H.,Randolph, P.H.,Bammes, B.,Stagg, S.M. (deposition date: 2022-09-14, release date: 2022-12-21, Last modification date: 2024-06-19)
Primary citationPeng, 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: 36578473
DOI: 10.1016/j.yjsbx.2022.100080
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.24 Å)
Structure validation

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