7KA2

Aldolase, rabbit muscle (beam-tilt refinement x2)

7KA2 の概要

• エントリーDOI: 10.2210/pdb7ka2/pdb
• EMDBエントリー: 22756
• 分子名称: Fructose-bisphosphate aldolase A (1 entity in total)
• 機能のキーワード: glycolysis, gluconeogenesis, carbohydrate degradation, homotetramer, lyase
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157054.69

構造登録者

Kearns, S.K.,Cash, J.N.,Cianfrocco, M.A.,Li, Y. (登録日: 2020-09-29, 公開日: 2020-12-02, 最終更新日: 2024-03-06)

主引用文献

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

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: 33209328
DOI: 10.1107/S2052252520013482

実験手法

ELECTRON MICROSCOPY (3.6 Å)