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Semi-automated selection of cryo-EM particles in RELION-1.3

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Scheres, Sjors H.W.·2015·Journal of Structural Biology

Abstract

The selection of particles suitable for high-resolution cryo-EM structure determination from noisy micrographs may represent a tedious and time-consuming step. Here, a semi-automated particle selection procedure is presented that has been implemented within the open-source software RELION. At the heart of the procedure lies a fully CTF-corrected template-based picking algorithm, which is supplemented by a fast sorting algorithm and reference-free 2D class averaging to remove false positives. With only limited user-interaction, the proposed procedure yields results that are comparable to manual particle selection. Together with an improved graphical user interface, these developments further contribute to turning RELION from a stand-alone refinement program into a convenient image processing pipeline for the entire single-particle approach.

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Research works printed but not linked: 39

  1. Allegretti, 2014, Atomic model of the f420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector, eLife, 3, 10.7554/eLife.01963 · DOI
  2. Amunts, 2014, Structure of the yeast mitochondrial large ribosomal subunit, Science, 343, 1485, 10.1126/science.1249410 · DOI · Paper page
  3. Bai, 2013, Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles, eLife, 2, e00461, 10.7554/eLife.00461 · DOI
  4. Campbell, 2012, Movies of ice-embedded particles enhance resolution in electron cryo-microscopy, Structure, 20, 1823, 10.1016/j.str.2012.08.026 · DOI · Paper page
  5. Cao, 2013, TRPV1 structures in distinct conformations reveal activation mechanisms, Nature, 504, 113, 10.1038/nature12823 · DOI
  6. Chen, 2007, SIGNATURE: a single-particle selection system for molecular electron microscopy, J. Struct. Biol., 157, 168, 10.1016/j.jsb.2006.06.001 · DOI
  7. Chen, 2013, High-resolution noise substitution to measure overfitting and validate resolution in 3d structure determination by single particle electron cryomicroscopy, Ultramicroscopy, 135, 24, 10.1016/j.ultramic.2013.06.004 · DOI
  8. Dugdale, 2010, Role of met-542 as a guide for the conformational changes of phe-601 that occur during the reaction of β-galactosidase (Escherichia coli), Biochem. Cell Biol., 88, 861, 10.1139/O10-009 · DOI
  9. Fernndez, 2013, Molecular architecture of a eukaryotic translational initiation complex, Science (New York, N.Y.), 342, 1240585, 10.1126/science.1240585 · DOI
  10. Grigorieff, 2011, Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy, Curr. Opin. Struct. Biol., 21, 265, 10.1016/j.sbi.2011.01.008 · DOI
  11. Hall, 1991, The STAR file: a new format for electronic data transfer and archiving, J. Chem. Inf. Comput. Sci., 31, 326, 10.1021/ci00002a020 · DOI
  12. Henderson, 2013, Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise, Proc. Natl. Acad. Sci. USA, 110, 18037, 10.1073/pnas.1314449110 · DOI
  13. Kucukelbir, 2014, Quantifying the local resolution of cryo-EM density maps, Nat. Methods, 11, 63, 10.1038/nmeth.2727 · DOI
  14. Langlois, 2011, A clarification of the terms used in comparing semi-automated particle selection algorithms in cryo-EM, J. Struct. Biol., 175, 348, 10.1016/j.jsb.2011.03.009 · DOI
  15. Langlois, 2014, Automated particle picking for low-contrast macromolecules in cryo-electron microscopy, J. Struct. Biol., 186, 1, 10.1016/j.jsb.2014.03.001 · DOI
  16. 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
  17. Lu, 2014, Three-dimensional structure of human-secretase, Nature, 512, 166, 10.1038/nature13567 · DOI
  18. McMullan, 2009, Detective quantum efficiency of electron area detectors in electron microscopy, Ultramicroscopy, 109, 1126, 10.1016/j.ultramic.2009.04.002 · DOI
  19. 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
  20. Nicholson, 2001, Review: automatic particle detection in electron microscopy, J. Struct. Biol., 133, 90, 10.1006/jsbi.2001.4348 · DOI
  21. Roseman, 2003, Particle finding in electron micrographs using a fast local correlation algorithm, Ultramicroscopy, 94, 225, 10.1016/S0304-3991(02)00333-9 · DOI
  22. Roseman, 2004, FindEM – a fast, efficient program for automatic selection of particles from electron micrographs, J. Struct. Biol., 145, 91, 10.1016/j.jsb.2003.11.007 · DOI
  23. Scheres, 2014, Beam-induced motion correction for sub-megadalton cryo-EM particles, eLife, 3, e03665, 10.7554/eLife.03665 · DOI
  24. Scheres, 2010, Classification of structural heterogeneity by maximum-likelihood methods, vol. 482, 295
  25. Scheres, 2012, A bayesian view on cryo-EM structure determination, J. Mol. Biol., 415, 406, 10.1016/j.jmb.2011.11.010 · DOI · Paper page
  26. Scheres, 2012, RELION: implementation of a bayesian approach to cryo-EM structure determination, J. Struct. Biol., 180, 519, 10.1016/j.jsb.2012.09.006 · DOI · Paper page
  27. Scheres, 2012, Prevention of overfitting in cryo-EM structure determination, Nat. Methods, 9, 853, 10.1038/nmeth.2115 · DOI · Paper page
  28. Scheres, 2007, Disentangling conformational states of macromolecules in 3d-EM through likelihood optimization, Nat. Methods, 4, 27, 10.1038/nmeth992 · DOI
  29. Shatsky, 2009, A method for the alignment of heterogeneous macromolecules from electron microscopy, J. Struct. Biol., 166, 67, 10.1016/j.jsb.2008.12.008 · DOI
  30. Sorzano, 2004, Normalizing projection images: a study of image normalizing procedures for single particle three-dimensional electron microscopy, Ultramicroscopy, 101, 129, 10.1016/j.ultramic.2004.04.004 · DOI
  31. Sorzano, 2009, Automatic particle selection from electron micrographs using machine learning techniques, J. Struct. Biol., 167, 252, 10.1016/j.jsb.2009.06.011 · DOI
  32. Suloway, 2005, Automated molecular microscopy: the new leginon system, J. Struct. Biol., 151, 41, 10.1016/j.jsb.2005.03.010 · DOI · Paper page
  33. Tang, 2007, EMAN2: an extensible image processing suite for electron microscopy, J. Struct. Biol., 157, 38, 10.1016/j.jsb.2006.05.009 · DOI
  34. van Heel, 2013, Finding trimeric HIV-1 envelope glycoproteins in random noise, Proc. Natl. Acad. Sci. USA, 110, E4175, 10.1073/pnas.1314353110 · DOI
  35. Vinothkumar, 2014, Molecular mechanism of antibody-mediated activation of galactosidase, Structure, 22, 621, 10.1016/j.str.2014.01.011 · DOI
  36. Voorhees, 2014, Structure of the mammalian ribosome-Sec61 complex to 3.4 resolution, Cell, 157, 1632, 10.1016/j.cell.2014.05.024 · DOI
  37. Voss, 2009, DoG picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy, J. Struct. Biol., 166, 205, 10.1016/j.jsb.2009.01.004 · DOI
  38. Wong, 2014, Cryo-EM structure of the Plasmodium falciparum 80s ribosome bound to the anti-protozoan drug emetine, eLife, e03080, 10.7554/eLife.03080 · DOI · Paper page
  39. Zhu, 2004, Automatic particle selection: results of a comparative study, J. Struct. Biol., 145, 3, 10.1016/j.jsb.2003.09.033 · DOI

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Metadata

Authors
Scheres, S. H. W.
Venue
Journal of Structural Biology
Publisher
Elsevier BV
Published
2015-02
Volume
189
Issue
2
Pages
114-122
ISSN
1047-8477 (ISSN-L)
OpenAlex
W1982295411
Cited by
377
References
0
FWCI
18.60
Type
journal article
Language
en
Open access
hybrid
Licence
Funders
UK Medical Research Council (MC_UP_A025_1013)

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CoChat. (2026). Citation check: Semi-automated selection of cryo-EM particles in RELION-1.3. https://app.cochat.ai/papers/10.1016/j.jsb.2014.11.010
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Scheres, S. H. W. (2015). Semi-automated selection of cryo-EM particles in RELION-1.3. Journal of Structural Biology. https://doi.org/10.1016/j.jsb.2014.11.010

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