7ka4

Aldolase, rabbit muscle (beam-tilt refinement x4)

spinqualitylabelsall models 7ka4, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A. After particle polishing and iterative rounds of aberration correction in RELION, a 2.8 A resolution structure could be obtained. This analysis demonstrates that software correction of microscope aberrations can provide a significant improvement in resolution at 200 keV. High-resolution cryo-EM using beam-image shift at 200 keV.,Cash JN, Kearns S, Li Y, Cianfrocco MA IUCrJ. 2020 Oct 29;7(Pt 6):1179-1187. doi: 10.1107/S2052252520013482. eCollection , 2020 Nov 1. PMID:33209328 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase 3D structures

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