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MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
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Abstract
MotionCor2 software corrects for beam-induced sample motion, improving the resolution of cryo-EM reconstructions.
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Kühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
Research works printed but not linked: 7
- Cheng, Y. Cell 161, 450–457 (2015). · DOI · Paper page
- Brilot, A.F. et al. J. Struct. Biol. 177, 630–637 (2012). · DOI · Paper page
- Li, X. et al. Nat. Methods 10, 584–590 (2013). · DOI · Paper page
- Liao, M., Cao, E., Julius, D. & Cheng, Y. Nature 504, 107–112 (2013). · DOI · Paper page
- Bai, X.C., Fernandez, I.S., McMullan, G. & Scheres, S.H. eLife 2, e00461 (2013). · DOI · Paper page
- Rubinstein, J.L. & Brubaker, M.A. J. Struct. Biol. 192, 188–195 (2015). · DOI · Paper page
- Grant, T. & Grigorieff, N. eLife 4, e06980 (2015). · DOI · Paper page
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Ferro, L. S., Fang, Q., Eshun-Wilson, L., Fernandes, J., Jack, A., Farrell, D. P., Golcuk, M., Huijben, T., Costa, K., Gur, M., et al. (2022) · Science · doi:10.1126/science.abf6154 · Cited by 112
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Gupta, M., Azumaya, C. M., Moritz, M., Pourmal, S., Diallo, A., Merz, G. E., Jang, G., Bouhaddou, M., Fossati, A., Brilot, A. F., et al. (2021) · doi:10.1101/2021.05.10.443524 · Cited by 89
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Long, H., Zheng, W., Liu, Y., Sun, Y., Zhao, K., Liu, Z., Xia, W., Lv, S., Liu, Z., Li, D., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012435118 · Cited by 60
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Kendall, A. K., Xie, B., Xu, P., Wang, J., Burcham, R., Frazier, M. N., Binshtein, E., Wei, H., Graham, T. R., Nakagawa, T., et al. (2020) · Structure · doi:10.1016/j.str.2020.01.009 · Cited by 57
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Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.011 · Cited by 55
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Snead, D. M., Matyszewski, M., Dickey, A. M., Lin, Y. X., Leschziner, A. E., & Reck-Peterson, S. L. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00863-y · Cited by 54
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Weijman, J. F., Yadav, S. K. N., Surridge, K. J., Cross, J. A., Borucu, U., Mantell, J., Woolfson, D. N., Schaffitzel, C., & Dodding, M. P. (2022) · Science Advances · doi:10.1126/sciadv.abp9660 · Cited by 54
Cryo-EM structure of the cytosolic AhR complex.
Wen, Z., Zhang, Y., Zhang, B., Hang, Y., Xu, L., Chen, Y., Xie, Q., Zhao, Q., Zhang, L., Li, G., et al. (2023) · Structure · doi:10.1016/j.str.2022.12.013 · Cited by 51
Conformational motions and ligand-binding underlying gating and regulation in IP3R channel
Fan, G., Baker, M. R., Terry, L. E., Arige, V., Chen, M., Seryshev, A. B., Baker, M. L., Ludtke, S. J., Yule, D. I., & Serysheva, I. I. (2022) · Nature Communications · doi:10.1038/s41467-022-34574-1 · Cited by 52
Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1
Rochon, K., Bauer, B. L., Roethler, N. A., Buckley, Y., Su, C.-C., Huang, W., Ramachandran, R., Stoll, M. S. K., Yu, E. W., Taylor, D. J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45524-4 · Cited by 52
Cryptochrome–Timeless structure reveals circadian clock timing mechanisms
Lin, C., Feng, S., DeOliveira, C. C., & Crane, B. R. (2023) · Nature · doi:10.1038/s41586-023-06009-4 · Cited by 51
Structure of ATP synthase under strain during catalysis
Guo, H., & Rubinstein, J. L. (2022) · Nature Communications · doi:10.1038/s41467-022-29893-2 · Cited by 51
Cryo-EM structure of a RAS/RAF recruitment complex
Park, E., Rawson, S., Schmoker, A., Kim, B.-W., Oh, S., Song, K., Jeon, H., & Eck, M. J. (2023) · Nature Communications · doi:10.1038/s41467-023-40299-6 · Cited by 51
Bahar, M. W., Porta, C., Fox, H., Macadam, A. J., Fry, E. E., & Stuart, D. I. (2021) · npj Vaccines · doi:10.1038/s41541-020-00267-3 · Cited by 42
Allosteric interactions prime androgen receptor dimerization and activation
Wasmuth, E. V., Broeck, A. V., LaClair, J. R., Hoover, E. A., Lawrence, K. E., Paknejad, N., Pappas, K., Matthies, D., Wang, B., Feng, W., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.035 · Cited by 50
“Frames were motion-corrected using MotionCor2 (Zheng et al., 2017) and the contrast transfer function estimated using CTFFIND4 (Rohou and Grigorieff, 2015).”
MethodStructural basis for lipid transfer by the ATG2A–ATG9A complex
(2024) · doi:10.1038/s41594-024-01376-6 · Cited by 50
Determinants shaping the nanoscale architecture of the mouse rod outer segment
Pöge, M., Mahamid, J., Imanishi, S. S., Plitzko, J. M., Palczewski, K., & Baumeister, W. (2021) · eLife · doi:10.7554/elife.72817 · Cited by 50
Partially inserted nascent chain unzips the lateral gate of the Sec translocon.
Kater, L., Frieg, B., Berninghausen, O., Gohlke, H., Beckmann, R., & Kedrov, A. (2019) · The EMBO Reports · doi:10.15252/embr.201948191 · Cited by 43
Kraushar, M. L., Krupp, F., Harnett, D., Turko, P., Ambrozkiewicz, M. C., Sprink, T., Imami, K., Günnigmann, M., Zinnall, U., Vieira-Vieira, C. H., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.11.037 · Cited by 49
Stokes, K., Winczura, A., Song, B., De Piccoli, G., & Grabarczyk, D. B. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa541 · Cited by 48
Structural determinants of microtubule minus end preference in CAMSAP CKK domains
Atherton, J., Luo, Y., Xiang, S., Yang, C., Rai, A., Jiang, K., Stangier, M., Vemu, A., Cook, A. D., Wang, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13247-6 · Cited by 48
Structures of BIRC6-client complexes provide a mechanism of SMAC-mediated release of caspases
Hunkeler, M., Jin, C. Y., & Fischer, E. S. (2023) · Science · doi:10.1126/science.ade5750 · Cited by 48
Metadata
- Authors
- Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A.
- Venue
- Nature Methods
- Published
- 2017-02-27
- Volume
- 14
- Issue
- 4
- Pages
- 331-332
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2593511418
- Cited by
- 7,777
- References
- 3
- FWCI
- 229.14
- Type
- journal article
- Language
- en
- Open access
- green
- Licence
- www.springer.com/tdm (tdm)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.