5. J.A.G. Briggs, Structural biology in situ–the potential of subtomogram averaging. Curr.
Opin. Struct. Biol. 23(2), 261–267 (2013)
6. W. Kühlbrandt, The resolution revolution. Science 343(6178), 1443–1444 (2014)
7. D.B. Williams, C.B. Carter, Transmission Electron Microscopy: A Textbook for Materials
Science. (Springer, 2009)
8. G. Rhodes, Crystallography made crystal clear a guide for users of macromolecular models
(Elsevier/Academic Press, Amsterdam; Boston, 2006)
9. E. Hecht, Optics (Fourth edition, Pearson new international edition, 2014)
10. J.C. Russ, The image processing handbook, 6th edn. (CRC; London, Boca Raton, Fla, 2010)
11. J. Dubochet, Cryo-EM—the first thirty years. J. Microsc. 245(3), 221–224 (2012)
12. K. Dierksen, D. Typke, R. Hegerl, J. Walz, E. Sackmann, W. Baumeister, Three-dimensional
structure of lipid vesicles embedded in vitreous ice and investigated by automated electron
tomography. Biophys. J. 68(4), 1416–1422 (1995)
13. R. Grimm, M. Bärmann, W. Häckl, D. Typke, E. Sackmann, W. Baumeister, Energy filtered
electron tomography of ice-embedded actin and vesicles. Biophys. J. 72(1), 482–489 (1997)
14. R. Grimm, H. Singh, R. Rachel, D. Typke, W. Zillig, W. Baumeister, Electron tomography
of ice-embedded prokaryotic cells. Biophys. J. 74(2), 1031–1042 (1998)
15. P.N.T. Unwin, P.D. Ennis, Two configurations of a channel-forming membrane protein.
Nature 307(5952), 609–613 (1984)
16. J. Dubochet, Aw McDowall, Vitrification of pure water for electron microscopy. J. Microsc.
124(3), 3–4 (1981)
17. L. Gan, M.S. Ladinsky, G.J. Jensen, Organization of the smallest eukaryotic spindle. Curr.
Biol. 21(18), 1578–1583 (2011)
18. M.M. Farley, B. Hu, W. Margolin, J. Liu, Minicells, Back in Fashion. J. Bacteriol. JB.
00901–15 (2016)
19. E.I. Tocheva et al., Peptidoglycan transformations during Bacillus subtilis sporulation. Mol.
Microbiol. 88(4), 673–686 (2013)
20. T. Murray, D.L. Popham, P. Setlow, Bacillus subtilis cells lacking penicillin-binding protein
1 require increased levels of divalent cations for growth. J. Bacteriol. 180(17), 4555–4563
(1998)
21. M. Schaechter, O. Maaloe, N. Kjeldgaard, Dependency on medium and temperature of cell
size and chemical composition during balanced grown of Salmonella typhimurium. J. Gen.
Microbiol. 19(3), 592–606 (1958)
22. S. Chen et al., Structural diversity of bacterial flagellar motors. EMBO J. 30(14), 2972–2981
(2011)
23. K.M. Davies et al., Macromolecular organization of ATP synthase and complex I in whole
mitochondria. Proc. Natl. Acad. Sci. 108(34), 14121–14126 (2011)
24. K.H. Bui et al., Integrated structural analysis of the human nuclear pore complex scaffold.
Cell 155(6), 1233–1243 (2013)
25. A. Briegel, et al., Structure of bacterial cytoplasmic chemoreceptor arrays and implications
for chemotactic signaling. eLife 3, e02151 ( 2014)
26. C.J. Russo, L.A. Passmore, Ultrastable gold substrates: properties of a support for
high-resolution electron cryomicroscopy of biological specimens. J. Struct. Biol. 193(1),
33–44 (2016)
27. W.F. Tivol, A. Briegel, G.J. Jensen, An improved cryogen for plunge freezing. Microsc.
Microanal. 14(05), 375–379 (2008)
28. D. Studer, B.M. Humbel, M. Chiquet, Electron microscopy of high pressure frozen samples:
bridging the gap between cellular ultrastructure and atomic resolution. Histochem. Cell Biol.
130(5), 877–889 (2008)
29. K.L. McDonald, M. Auer, High-pressure freezing, cellular tomography, and structural cell
biology, BioTechniques, 41(2), 137, 139, 141 passim, (Aug. 2006)
30. M. Marko, C. Hsieh, W. Moberlychan, C.A. Mannella, J. Frank, Focused ion beam milling
of vitreous water: prospects for an alternative to cryo-ultramicrotomy of frozen-hydrated
biological samples. J. Microsc. 222(1), 42–47 (2006)
3 Electron Cryo-Tomography
89
Opin. Struct. Biol. 23(2), 261–267 (2013)
6. W. Kühlbrandt, The resolution revolution. Science 343(6178), 1443–1444 (2014)
7. D.B. Williams, C.B. Carter, Transmission Electron Microscopy: A Textbook for Materials
Science. (Springer, 2009)
8. G. Rhodes, Crystallography made crystal clear a guide for users of macromolecular models
(Elsevier/Academic Press, Amsterdam; Boston, 2006)
9. E. Hecht, Optics (Fourth edition, Pearson new international edition, 2014)
10. J.C. Russ, The image processing handbook, 6th edn. (CRC; London, Boca Raton, Fla, 2010)
11. J. Dubochet, Cryo-EM—the first thirty years. J. Microsc. 245(3), 221–224 (2012)
12. K. Dierksen, D. Typke, R. Hegerl, J. Walz, E. Sackmann, W. Baumeister, Three-dimensional
structure of lipid vesicles embedded in vitreous ice and investigated by automated electron
tomography. Biophys. J. 68(4), 1416–1422 (1995)
13. R. Grimm, M. Bärmann, W. Häckl, D. Typke, E. Sackmann, W. Baumeister, Energy filtered
electron tomography of ice-embedded actin and vesicles. Biophys. J. 72(1), 482–489 (1997)
14. R. Grimm, H. Singh, R. Rachel, D. Typke, W. Zillig, W. Baumeister, Electron tomography
of ice-embedded prokaryotic cells. Biophys. J. 74(2), 1031–1042 (1998)
15. P.N.T. Unwin, P.D. Ennis, Two configurations of a channel-forming membrane protein.
Nature 307(5952), 609–613 (1984)
16. J. Dubochet, Aw McDowall, Vitrification of pure water for electron microscopy. J. Microsc.
124(3), 3–4 (1981)
17. L. Gan, M.S. Ladinsky, G.J. Jensen, Organization of the smallest eukaryotic spindle. Curr.
Biol. 21(18), 1578–1583 (2011)
18. M.M. Farley, B. Hu, W. Margolin, J. Liu, Minicells, Back in Fashion. J. Bacteriol. JB.
00901–15 (2016)
19. E.I. Tocheva et al., Peptidoglycan transformations during Bacillus subtilis sporulation. Mol.
Microbiol. 88(4), 673–686 (2013)
20. T. Murray, D.L. Popham, P. Setlow, Bacillus subtilis cells lacking penicillin-binding protein
1 require increased levels of divalent cations for growth. J. Bacteriol. 180(17), 4555–4563
(1998)
21. M. Schaechter, O. Maaloe, N. Kjeldgaard, Dependency on medium and temperature of cell
size and chemical composition during balanced grown of Salmonella typhimurium. J. Gen.
Microbiol. 19(3), 592–606 (1958)
22. S. Chen et al., Structural diversity of bacterial flagellar motors. EMBO J. 30(14), 2972–2981
(2011)
23. K.M. Davies et al., Macromolecular organization of ATP synthase and complex I in whole
mitochondria. Proc. Natl. Acad. Sci. 108(34), 14121–14126 (2011)
24. K.H. Bui et al., Integrated structural analysis of the human nuclear pore complex scaffold.
Cell 155(6), 1233–1243 (2013)
25. A. Briegel, et al., Structure of bacterial cytoplasmic chemoreceptor arrays and implications
for chemotactic signaling. eLife 3, e02151 ( 2014)
26. C.J. Russo, L.A. Passmore, Ultrastable gold substrates: properties of a support for
high-resolution electron cryomicroscopy of biological specimens. J. Struct. Biol. 193(1),
33–44 (2016)
27. W.F. Tivol, A. Briegel, G.J. Jensen, An improved cryogen for plunge freezing. Microsc.
Microanal. 14(05), 375–379 (2008)
28. D. Studer, B.M. Humbel, M. Chiquet, Electron microscopy of high pressure frozen samples:
bridging the gap between cellular ultrastructure and atomic resolution. Histochem. Cell Biol.
130(5), 877–889 (2008)
29. K.L. McDonald, M. Auer, High-pressure freezing, cellular tomography, and structural cell
biology, BioTechniques, 41(2), 137, 139, 141 passim, (Aug. 2006)
30. M. Marko, C. Hsieh, W. Moberlychan, C.A. Mannella, J. Frank, Focused ion beam milling
of vitreous water: prospects for an alternative to cryo-ultramicrotomy of frozen-hydrated
biological samples. J. Microsc. 222(1), 42–47 (2006)
3 Electron Cryo-Tomography
89