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Methods Development


A major interest of the lab is the development and optimisation of methods for high-resolution cryo-EM. This has led us to investigate


  1. Grigorieff, N.  2007.  FREALIGN: high-resolution refinement of single particle structures. J Struct Biol. 157:117–125.
  2. Grigorieff, N.  1998.  Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice. J Mol Biol. 277:1033-46.
  3. Wolf, M, DeRosier DJ, Grigorieff N.  2006.  Ewald sphere correction for single-particle electron microscopy. Ultramicroscopy. 106:376-82.
  4. Stewart, A, Grigorieff N.  2004.  Noise bias in the refinement of structures derived from single particles. Ultramicroscopy. 102:67-84.
  5. Chen, JZ, Grigorieff N.  2007.  SIGNATURE: a single-particle selection system for molecular electron microscopy. J Struct Biol. 157:168-73.
  6. Grigorieff, N.  2000.  Resolution measurement in structures derived from single particles. Acta Crystallogr D Biol Crystallogr. 56:1270-7.
  7. Sousa, D, Grigorieff N.  2007.  Ab initio resolution measurement for single particle structures. J Struct Biol. 157:201-10.
  8. Sachse, C, Chen JZ, Coureux PD, Stroupe ME, Fändrich M, Grigorieff N.  2007.  High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J Mol Biol. 371:812-35.
  9. Rohou, A, Grigorieff N.  2014.  Frealix: model-based refinement of helical filament structures from electron micrographs. J Struct Biol. 186:234–244.
  10. Mindell, JA, Grigorieff N.  2003.  Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol. 142:334-47.
  11. Rohou, A, Grigorieff N.  2015.  CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J Struct Biol. 192:216–221.
  12. Ruskin, RS, Yu Z, Grigorieff N.  2013.  Quantitative characterization of electron detectors for transmission electron microscopy. J Struct Biol. 184:385-393.
  13. Brilot, AF, Chen JZ, Cheng A, Pan J, Harrison SC, Potter CS, Carragher B, Henderson R, Grigorieff N.  2012.  Beam-induced motion of vitrified specimen on holey carbon film.. J Struct Biol. 177:630-637.
  14. Campbell, MG, Cheng A, Brilot AF, Moeller A, Lyumkis D, Veesler D, Pan J, Harrison SC, Potter CS, Carragher B et al..  2012.  Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. Structure. 20:1823–1828.
  15. Grant, T, Grigorieff N.  2015.  Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6. eLife. 4(e06980):1-19.
  16. Grant, T, Grigorieff N.  2015.  Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J Struct Biol. 192:204–208.
  17. Lyumkis, D, Brilot AF, Theobald DL, Grigorieff N.  2013.  Likelihood-based classification of cryo-EM images using FREALIGN. J Struct Biol. 183:377-388.
  18. Grigorieff, N.  2016.  Frealign: An exploratory tool for single-particle cryo-EM. Methods in Enzymology. 579:191-226.
  19. Rickgauer, JP, Grigorieff N, Denk W.  2017.  Single-protein detection in crowded molecular environments in cryo-EM images. eLife. 6(e25648):1-22.
  20. Grant, T, Rohou A, Grigorieff N.  2018.  cisTEM, User-friendly software for single-particle image processing. eLife. 7(e35383)