48. M. Eibauer, C. Hoffmann, J.M. Plitzko, W. Baumeister, S. Nickell, H. Engelhardt, Unraveling
the structure of membrane proteins in situ by transfer function corrected cryo-electron
tomography. J. Struct. Biol. 180(3), 488–496 (2012)
49. L.M. Voortman et al., Quantifying resolution limiting factors in subtomogram averaged
cryo-electron tomography using simulations. J. Struct. Biol. 187(2), 103–111 (2014)
50. Q. Yang, Y. Wang, Q. Liu, X. Yan, An accurate analytical approach to electron
crystallography. Ultramicroscopy 87(4), 177–186 (2001)
51. M.C. Scott et al., Electron tomography at 2.4-ångström resolution. Nature 483(7390), 444–
447 (2012)
52. J. Miao, F. Förster, O. Levi, Equally sloped tomography with oversampling reconstruction.
Phys. Rev. B 72(5), 52103 (2005)
53. S.G. Wolf, L. Houben, M. Elbaum, Cryo-scanning transmission electron tomography of
vitrified cells. Nat. Methods 11(4), 423–428 (2014)
54. G. Cardone, K. Grünewald, A.C. Steven, A resolution criterion for electron tomography based
on cross-validation. J. Struct. Biol. 151(2), 117–129 (2005)
55. N.V. Dudkina, M. Kudryashev, H. Stahlberg, E.J. Boekema, Interaction of complexes I, III,
and IV within the bovine respirasome by single particle cryoelectron tomography. Proc. Natl.
Acad. Sci. U. S. A. 108(37), 15196–15200 (2011)
56. C.A. Diebolder, F.G.A. Faas, A.J. Koster, R.I. Koning, Conical Fourier shell correlation
applied to electron tomograms. J. Struct. Biol. 190(2), 215–223 (2015)
57. H. Heidari Mezerji, W. Van den Broek, S. Bals, A practical method to determine the effective
resolution in incoherent experimental electron tomography. Ultramicroscopy 111(5), 330–336
(2011)
58. L.G. Trabuco, E. Villa, K. Mitra, J. Frank, K. Schulten, “Flexible fitting of atomic structures
into electron microscopy maps using molecular dynamics,” Struct. Lond. Engl. 1993 16(5),
673–683 (2008)
59. F.K.M. Schur et al., Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å
resolution. Nature 517(7535), 505–508 (2015)
60. S. Pfeffer et al., Structure of the native Sec61 protein-conducting channel. Nat. Commun. 6,
8403 (2015)
61. A. Bartesaghi, F. Lecumberry, G. Sapiro, S. Subramaniam, “Protein secondary structure
determination by constrained single-particle cryo-electron tomography,” Struct. Lond. Engl.
1993 20(12), 2003–2013 (2012)
62. F.K.M. Schur, R.A. Dick, W.J.H. Hagen, V.M. Vogt, J.A.G. Briggs, The Structure of
Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10
Domain in Assembly. J. Virol. 89(20), 10294–10302 (2015)
63. T.A.M. Bharat, C.J. Russo, J. Löwe, L.A. Passmore, S.H.W. Scheres, “Advances in
Single-Particle Electron Cryomicroscopy Structure Determination applied to Sub-tomogram
Averaging,” Struct. Lond. Engl. 1993 23(9), 1743–1753 (2015)
64. M. Kudryashev et al., “The Structure of the Mouse Serotonin 5-HT3 Receptor in Lipid
Vesicles,” Struct. Lond. Engl. 1993 24(1), 165–170 (2016)
65. M. Kunz, A.S. Frangakis, “Three-dimensional CTF correction improves the resolution of
electron tomograms,” J. Struct. Biol. (2016)
66. W.J.H. Hagen, W. Wan, J.A.G. Briggs, “Implementation of a cryo-electron tomography
tilt-scheme optimized for high resolution subtomogram averaging,” J. Struct. Biol. (2016)
67. F.K.M. Schur et al., An atomic model of HIV-1 capsid-SP1 reveals structures regulating
assembly and maturation. Science 353(6298), 506–508 (2016)
68. G.J. Jensen, Alignment error envelopes for single particle analysis. J. Struct. Biol. 133(2–3),
143–155 (2001)
69. J.M. Spear, A.J. Noble, Q. Xie, D.R. Sousa, M.S. Chapman, S.M. Stagg, The influence of
frame alignment with dose compensation on the quality of single particle reconstructions.
J. Struct. Biol. 192(2), 196–203 (2015)
70. S.H.W. Scheres, S. Chen, Prevention of overfitting in cryo-EM structure determination. Nat.
Methods 9(9), 853–854 (2012)
10 Resolution in Electron Tomography
281
the structure of membrane proteins in situ by transfer function corrected cryo-electron
tomography. J. Struct. Biol. 180(3), 488–496 (2012)
49. L.M. Voortman et al., Quantifying resolution limiting factors in subtomogram averaged
cryo-electron tomography using simulations. J. Struct. Biol. 187(2), 103–111 (2014)
50. Q. Yang, Y. Wang, Q. Liu, X. Yan, An accurate analytical approach to electron
crystallography. Ultramicroscopy 87(4), 177–186 (2001)
51. M.C. Scott et al., Electron tomography at 2.4-ångström resolution. Nature 483(7390), 444–
447 (2012)
52. J. Miao, F. Förster, O. Levi, Equally sloped tomography with oversampling reconstruction.
Phys. Rev. B 72(5), 52103 (2005)
53. S.G. Wolf, L. Houben, M. Elbaum, Cryo-scanning transmission electron tomography of
vitrified cells. Nat. Methods 11(4), 423–428 (2014)
54. G. Cardone, K. Grünewald, A.C. Steven, A resolution criterion for electron tomography based
on cross-validation. J. Struct. Biol. 151(2), 117–129 (2005)
55. N.V. Dudkina, M. Kudryashev, H. Stahlberg, E.J. Boekema, Interaction of complexes I, III,
and IV within the bovine respirasome by single particle cryoelectron tomography. Proc. Natl.
Acad. Sci. U. S. A. 108(37), 15196–15200 (2011)
56. C.A. Diebolder, F.G.A. Faas, A.J. Koster, R.I. Koning, Conical Fourier shell correlation
applied to electron tomograms. J. Struct. Biol. 190(2), 215–223 (2015)
57. H. Heidari Mezerji, W. Van den Broek, S. Bals, A practical method to determine the effective
resolution in incoherent experimental electron tomography. Ultramicroscopy 111(5), 330–336
(2011)
58. L.G. Trabuco, E. Villa, K. Mitra, J. Frank, K. Schulten, “Flexible fitting of atomic structures
into electron microscopy maps using molecular dynamics,” Struct. Lond. Engl. 1993 16(5),
673–683 (2008)
59. F.K.M. Schur et al., Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å
resolution. Nature 517(7535), 505–508 (2015)
60. S. Pfeffer et al., Structure of the native Sec61 protein-conducting channel. Nat. Commun. 6,
8403 (2015)
61. A. Bartesaghi, F. Lecumberry, G. Sapiro, S. Subramaniam, “Protein secondary structure
determination by constrained single-particle cryo-electron tomography,” Struct. Lond. Engl.
1993 20(12), 2003–2013 (2012)
62. F.K.M. Schur, R.A. Dick, W.J.H. Hagen, V.M. Vogt, J.A.G. Briggs, The Structure of
Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10
Domain in Assembly. J. Virol. 89(20), 10294–10302 (2015)
63. T.A.M. Bharat, C.J. Russo, J. Löwe, L.A. Passmore, S.H.W. Scheres, “Advances in
Single-Particle Electron Cryomicroscopy Structure Determination applied to Sub-tomogram
Averaging,” Struct. Lond. Engl. 1993 23(9), 1743–1753 (2015)
64. M. Kudryashev et al., “The Structure of the Mouse Serotonin 5-HT3 Receptor in Lipid
Vesicles,” Struct. Lond. Engl. 1993 24(1), 165–170 (2016)
65. M. Kunz, A.S. Frangakis, “Three-dimensional CTF correction improves the resolution of
electron tomograms,” J. Struct. Biol. (2016)
66. W.J.H. Hagen, W. Wan, J.A.G. Briggs, “Implementation of a cryo-electron tomography
tilt-scheme optimized for high resolution subtomogram averaging,” J. Struct. Biol. (2016)
67. F.K.M. Schur et al., An atomic model of HIV-1 capsid-SP1 reveals structures regulating
assembly and maturation. Science 353(6298), 506–508 (2016)
68. G.J. Jensen, Alignment error envelopes for single particle analysis. J. Struct. Biol. 133(2–3),
143–155 (2001)
69. J.M. Spear, A.J. Noble, Q. Xie, D.R. Sousa, M.S. Chapman, S.M. Stagg, The influence of
frame alignment with dose compensation on the quality of single particle reconstructions.
J. Struct. Biol. 192(2), 196–203 (2015)
70. S.H.W. Scheres, S. Chen, Prevention of overfitting in cryo-EM structure determination. Nat.
Methods 9(9), 853–854 (2012)
10 Resolution in Electron Tomography
281