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-Structure paper
タイトル | High-resolution cryo-EM using beam-image shift at 200 keV. |
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ジャーナル・号・ページ | IUCrJ, Vol. 7, Issue Pt 6, Page 1179-1187, Year 2020 |
掲載日 | 2020年11月1日 |
著者 | Jennifer N Cash / Sarah Kearns / Yilai Li / Michael A Cianfrocco / |
PubMed 要旨 | 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 ...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. |
リンク | IUCrJ / PubMed:33209328 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.8 - 4.9 Å |
構造データ | EMDB-22754, PDB-7k9l: EMDB-22755, PDB-7k9x: EMDB-22756, PDB-7ka2: EMDB-22757, PDB-7ka3: EMDB-22758, PDB-7ka4: |
由来 |
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キーワード | LYASE / glycolysis / gluconeogenesis / Carbohydrate degradation / Homotetramer |