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Gctf: Real-time CTF determination and correction
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Abstract
Accurate estimation of the contrast transfer function (CTF) is critical for a near-atomic resolution cryo electron microscopy (cryoEM) reconstruction. Here, a GPU-accelerated computer program, Gctf, for accurate and robust, real-time CTF determination is presented. The main target of Gctf is to maximize the cross-correlation of a simulated CTF with the logarithmic amplitude spectra (LAS) of observed micrographs after background subtraction. Novel approaches in Gctf improve both speed and accuracy. In addition to GPU acceleration (e.g. 10-50×), a fast '1-dimensional search plus 2-dimensional refinement (1S2R)' procedure further speeds up Gctf. Based on the global CTF determination, the local defocus for each particle and for single frames of movies is accurately refined, which improves CTF parameters of all particles for subsequent image processing. Novel diagnosis method using equiphase averaging (EPA) and self-consistency verification procedures have also been implemented in the program for practical use, especially for aims of near-atomic reconstruction. Gctf is an independent program and the outputs can be easily imported into other cryoEM software such as Relion (Scheres, 2012) and Frealign (Grigorieff, 2007). The results from several representative datasets are shown and discussed in this paper.
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Cites
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
Xu, W., Xu, F., Jones, M., Keszthelyi, B., Sedat, J., Agard, D., & Mueller, K. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.03.018 · Cited by 71
Li, X., Grigorieff, N., & Cheng, Y. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.06.010 · Cited by 45
Research works printed but not linked: 34
- Amunts, 2015, Ribosome. The structure of the human mitochondrial ribosome, Science, 348, 95, 10.1126/science.aaa1193 · DOI · Paper page
- Bai, 2015, How cryo-EM is revolutionizing structural biology, Trends Biochem. Sci., 40, 49, 10.1016/j.tibs.2014.10.005 · DOI · Paper page
- Bai, 2013, Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles, Elife, 2, e00461, 10.7554/eLife.00461 · DOI · Paper page
- Bartesaghi, 2015, 2.2Å resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor, Science, 10.1126/science.aab1576 · DOI · Paper page
- Brown, 2015, Structural basis for stop codon recognition in eukaryotes, Nature, 10.1038/nature14896 · DOI · Paper page
- DeRosier, 2000, Correction of high-resolution data for curvature of the Ewald sphere, Ultramicroscopy, 81, 83, 10.1016/S0304-3991(99)00120-5 · DOI
- Glaeser, 2011, Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM, J. Struct. Biol., 174, 1, 10.1016/j.jsb.2010.12.005 · DOI
- Grigorieff, 2007, FREALIGN: high-resolution refinement of single particle structures, J. Struct. Biol., 157, 117, 10.1016/j.jsb.2006.05.004 · DOI · Paper page
- Heymann, 2005, Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology, J. Struct. Biol., 151, 196, 10.1016/j.jsb.2005.06.001 · DOI
- Jiang, 2015, Atomic structure of anthrax protective antigen pore elucidates toxin translocation, Nature, 10.1038/nature14247 · DOI · Paper page
- Li, 2013, Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM, Nat. Methods, 10, 584, 10.1038/nmeth.2472 · DOI · Paper page
- Ludtke, 1999, EMAN: semiautomated software for high-resolution single-particle reconstructions, J. Struct. Biol., 128, 82, 10.1006/jsbi.1999.4174 · DOI · Paper page
- Mallick, 2005, ACE: automated CTF estimation, Ultramicroscopy, 104, 8, 10.1016/j.ultramic.2005.02.004 · DOI
- Marabini, 2015, CTF challenge: result summary, J. Struct. Biol., 10.1016/j.jsb.2015.04.003 · DOI
- Mindell, 2003, Accurate determination of local defocus and specimen tilt in electron microscopy, J. Struct. Biol., 142, 334, 10.1016/S1047-8477(03)00069-8 · DOI · Paper page
- Nogales, 2015, Cryo-EM: a unique tool for the visualization of macromolecular complexity, Mol. Cell, 58, 677, 10.1016/j.molcel.2015.02.019 · DOI · Paper page
- Paulsen, 2015, Structure of the TRPA1 ion channel suggests regulatory mechanisms, Nature, 520, 511, 10.1038/nature14367 · DOI · Paper page
- Penczek, 2014, CTER-rapid estimation of CTF parameters with error assessment, Ultramicroscopy, 140, 9, 10.1016/j.ultramic.2014.01.009 · DOI
- Rohou, 2015, CTFFIND4: fast and accurate defocus estimation from electron micrographs, J. Struct. Biol., 10.1016/j.jsb.2015.08.008 · DOI · Paper page
- Russo, 2014, Electron microscopy: ultrastable gold substrates for electron cryomicroscopy, Science, 346, 1377, 10.1126/science.1259530 · DOI · Paper page
- Shaikh, 2008, SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs, Nat. Protoc., 3, 1941, 10.1038/nprot.2008.156 · DOI · Paper page
- Shatsky, 2014, Automated particle correspondence and accurate tilt-axis detection in tilted-image pairs, J. Struct. Biol., 187, 66, 10.1016/j.jsb.2014.03.017 · DOI
- Sorzano, 2004, XMIPP: a new generation of an open-source image processing package for electron microscopy, J. Struct. Biol., 148, 194, 10.1016/j.jsb.2004.06.006 · DOI · Paper page
- Tang, 2007, EMAN2: an extensible image processing suite for electron microscopy, J. Struct. Biol., 157, 38, 10.1016/j.jsb.2006.05.009 · DOI · Paper page
- Taylor, 2015, Structural biology. Structures of the CRISPR-Cmr complex reveal mode of RNA target positioning, Science, 348, 581, 10.1126/science.aaa4535 · DOI
- Urnavicius, 2015, The structure of the dynactin complex and its interaction with dynein, Science, 347, 1441, 10.1126/science.aaa4080 · DOI · Paper page
- Vargas, 2013, FASTDEF: fast defocus and astigmatism estimation for high-throughput transmission electron microscopy, J. Struct. Biol., 181, 136, 10.1016/j.jsb.2012.12.006 · DOI
- Voortman, 2011, A fast algorithm for computing and correcting the CTF for tilted, thick specimens in TEM, Ultramicroscopy, 111, 1029, 10.1016/j.ultramic.2011.03.001 · DOI
- Wade, 1992, A brief look at imaging and contrast transfer, Ultramicroscopy, 46, 145, 10.1016/0304-3991(92)90011-8 · DOI
- Wang, 2015, Hepatitis A virus and the origins of picornaviruses, Nature, 517, 85, 10.1038/nature13806 · DOI
- Zhang, 2013, Flexible interwoven termini determine the thermal stability of thermosomes, Protein Cell, 4, 432, 10.1007/s13238-013-3026-9 · DOI
- Zhao, 2014, G-BLASTN: accelerating nucleotide alignment by graphics processors, Bioinformatics, 30, 1384, 10.1093/bioinformatics/btu047 · DOI
- Zhao, 2015, Mechanistic insights into the recycling machine of the SNARE complex, Nature, 518, 61, 10.1038/nature14148 · DOI
- Zhu, 2015, Structure of Ljungan virus provides insight into genome packaging of this picornavirus, Nat. Commun., 6, 8316, 10.1038/ncomms9316 · DOI
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Khalifa, A. A. Z., Ichikawa, M., Dai, D., Kubo, S., Black, C. S., Peri, K., McAlear, T. S., Veyron, S., Yang, S. K., Vargas, J., et al. (2020) · eLife · doi:10.7554/elife.52760 · Cited by 1,676
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Cao, Y., Su, B., Guo, X., Sun, W., Deng, Y., Bao, L., Zhu, Q., Zhang, X., Zheng, Y., Geng, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.025 · Cited by 1,188
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Zhang, S., Chang, L., Alfieri, C., Zhang, Z., Yang, J., Maslen, S., Skehel, M., & Barford, D. (2016) · Nature · doi:10.1038/nature17973 · Cited by 203
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Morreale, F. E., Kleine, S., Leodolter, J., Junker, S., Hoi, D. M., Ovchinnikov, S., Okun, A., Kley, J., Kurzbauer, R., Junk, L., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.009 · Cited by 196
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Yang, G., Zhou, R., Guo, X., Yan, C., Lei, J., & Shi, Y. (2021) · Cell · doi:10.1016/j.cell.2020.11.049 · Cited by 189
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Chen, Q., Plasencia, M., Li, Z., Mukherjee, S., Patra, D., Chen, C.-L., Klose, T., Yao, X.-Q., Kossiakoff, A. A., Chang, L., et al. (2021) · Nature · doi:10.1038/s41586-021-03721-x · Cited by 152
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Matsuo, Y., Tesina, P., Nakajima, S., Mizuno, M., Endo, A., Buschauer, R., Cheng, J., Shounai, O., Ikeuchi, K., Saeki, Y., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0393-9 · Cited by 150
Zhao, F., Zhou, Q., Cong, Z., Hang, K., Zou, X., Zhang, C., Chen, Y., Dai, A., Liang, A., Ming, Q., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28683-0 · Cited by 149
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Schumacher, S., Dedden, D., Nunez, R. V., Matoba, K., Takagi, J., Biertümpfel, C., & Mizuno, N. (2021) · Science Advances · doi:10.1126/sciadv.abe9716 · Cited by 150
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Chang, A., Xiang, X., Wang, J., Lee, C., Arakhamia, T., Simjanoska, M., Wang, C., Carlomagno, Y., Zhang, G., Dhingra, S., et al. (2022) · Cell · doi:10.1016/j.cell.2022.02.026 · Cited by 150
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Coscia, F., Taler-Verčič, A., Chang, V. T., Sinn, L., O’Reilly, F. J., Izoré, T., Renko, M., Berger, I., Rappsilber, J., Turk, D., et al. (2020) · Nature · doi:10.1038/s41586-020-1995-4 · Cited by 147
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Anandapadamanaban, M., Masson, G. R., Perisic, O., Berndt, A., Kaufman, J., Johnson, C. M., Santhanam, B., Rogala, K. B., Sabatini, D. M., & Williams, R. L. (2019) · Science · doi:10.1126/science.aax3939 · Cited by 147
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Wang, L., Qian, H., Nian, Y., Han, Y., Ren, Z., Zhang, H., Hu, L., Prasad, B. V. V., Laganowsky, A., Yan, N., et al. (2020) · Nature · doi:10.1038/s41586-020-2280-2 · Cited by 123
Bloch, J. S., Mukherjee, S., Kowal, J., Filippova, E. V., Niederer, M., Pardon, E., Steyaert, J., Kossiakoff, A. A., & Locher, K. P. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2115435118 · Cited by 114
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Cook, N. J., Li, W., Berta, D., Badaoui, M., Ballandras-Colas, A., Nans, A., Kotecha, A., Rosta, E., Engelman, A. N., & Cherepanov, P. (2020) · Science · doi:10.1126/science.aay4919 · Cited by 108
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Geng, J., Liu, W., Zhou, H., Zhang, T., Wang, L., Zhang, M., Li, Y., Shen, B., Li, X., & Xiao, B. (2020) · Neuron · doi:10.1016/j.neuron.2020.02.010 · Cited by 113
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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Lim, C. J., Barbour, A. T., Zaug, A. J., Goodrich, K. J., McKay, A. E., Wuttke, D. S., & Cech, T. R. (2020) · Science · doi:10.1126/science.aaz9649 · Cited by 111
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Qian, H., Zhao, X., Yan, R., Yao, X., Gao, S., Sun, X., Du, X., Yang, H., Wong, C. C. L., & Yan, N. (2020) · Nature · doi:10.1038/s41586-020-2290-0 · Cited by 108
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Twomey, E. C., Yelshanskaya, M. V., Vassilevski, A. A., & Sobolevsky, A. I. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.027 · Cited by 106
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Scaiola, A., Mangia, F., Imseng, S., Boehringer, D., Berneiser, K., Shimobayashi, M., Stuttfeld, E., Hall, M. N., Ban, N., & Maier, T. (2020) · Science Advances · doi:10.1126/sciadv.abc1251 · Cited by 105
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Huang, C.-S., Yu, X., Fordstrom, P., Choi, K., Chung, B. C., Roh, S.-H., Chiu, W., Zhou, M., Min, X., & Wang, Z. (2020) · Science Advances · doi:10.1126/sciadv.abb1989 · Cited by 98
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Cai, S., Wu, Y., Guillén-Samander, A., Hancock-Cerutti, W., Liu, J., & De Camilli, P. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2203769119 · Cited by 93
Kubo, S., Black, C. S., Joachimiak, E., Yang, S. K., Legal, T., Peri, K., Khalifa, A. A. Z., Ghanaeian, A., McCafferty, C. L., Valente-Paterno, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37868-0 · Cited by 93
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Walden, M., Tian, L., Ross, R. L., Sykora, U. M., Byrne, D. P., Hesketh, E. L., Masandi, S. K., Cassel, J., George, R., Ault, J. R., et al. (2019) · Nature · doi:10.1038/s41586-019-1232-1 · Cited by 85
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Pan, Y., Ren, Z., Gao, S., Shen, J., Wang, L., Xu, Z., Yu, Y., Bachina, P., Zhang, H., Fan, X., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19458-6 · Cited by 81
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Meyer, N. L., Hu, G., Davulcu, O., Xie, Q., Noble, A. J., Yoshioka, C., Gingerich, D. S., Trzynka, A., David, L., Stagg, S. M., et al. (2019) · eLife · doi:10.7554/elife.44707 · Cited by 83
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Chaaban, S., Jariwala, S., Hsu, C.-T., Redemann, S., Kollman, J. M., Müller-Reichert, T., Sept, D., Bui, K. H., & Brouhard, G. J. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.08.023 · Cited by 83
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Ding, B., Yang, S., Schaks, M., Liu, Y., Brown, A. J., Rottner, K., Chowdhury, S., & Chen, B. (2022) · Nature Communications · doi:10.1038/s41467-022-33174-3 · Cited by 82
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Yu, X., Matico, R. E., Miller, R., Chauhan, D., Van Schoubroeck, B., Grauwen, K., Suarez, J., Pietrak, B., Haloi, N., Yin, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45396-8 · Cited by 78
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Xue, J., Xie, T., Zeng, W., Jiang, Y., & Bai, X.-C. (2020) · eLife · doi:10.7554/elife.58823 · Cited by 78
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Metadata
- Authors
- Zhang, K.
- Venue
- Journal of Structural Biology
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 193
- Issue
- 1
- Pages
- 1-12
- ISSN
- 1047-8477 (ISSN-L)
- OpenAlex
- W2950967305
- Cited by
- 3,537
- References
- 3
- FWCI
- 61.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor)
- Funders
- Medical Research Council (MC_UP_A025_1011)
- Wellcome Trust New Investigator Award (WT100387)
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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.