75. L.A. Baker, J.L. Rubinstein, Radiation damage in electron cryomicroscopy. Methods
Enzymol. 481, 371–388 (2010). doi:10.1016/S0076-6879(10)81015-8
76. J.P. Buban, Q. Ramasse, B. Gipson, N.D. Browning, H. Stahlberg, High-resolution low-dose
scanning transmission electron microscopy. J. Electron. Microsc. (Tokyo) 59(2), 103–112
(2010). doi:10.1093/jmicro/dfp052
77. R.C. Guerrero-Ferreira, E.R. Wright, Cryo-electron tomography of bacterial viruses.
Virology 435(1), 179–186 (2013). doi:http://dx.doi.org/10.1016/j.virol.2012.08.022
78. K. Celler, R.I. Koning, A.J. Koster, G.P. van Wezel, Multidimensional view of the bacterial
cytoskeleton. J. Bacteriol. 195(8), 1627–1636 (2013). doi:10.1128/jb.02194-12
79. C.M. Oikonomou, G.J. Jensen, A new view into prokaryotic cell biology from electron
cryotomography. Nat. Rev. Micro. 14(4), 205–220 (2016). doi:10.1038/nrmicro.2016.7
80. V. Gold, M. Kudryashev, Recent progress in structure and dynamics of
dual-membrane-spanning bacterial nanomachines. Curr. Opin. Struct. Biol. 39, 1–7
(2016). doi:http://dx.doi.org/10.1016/j.sbi.2016.03.001
81. M.M. Farley, B. Hu, W. Margolin, J. Liu, Minicells, back in fashion. J. Bacteriol. 198(8),
1186–1195 (2016). doi:10.1128/jb.00901-15
82. X. Fu, B.A. Himes, D. Ke, W.J. Rice, J. Ning, P. Zhang, Controlled bacterial lysis for
electron tomography of native cell membranes. Structure 22(12), 1875–1882 (2014). doi:
http://dx.doi.org/10.1016/j.str.2014.09.017
83. P. Rez, W. Chiu, J.K. Weiss, J. Brink, The thickness determination of organic crystals under
low dose conditions using electron energy loss spectroscopy. Microsc. Res. Tech. 21(2),
166–170 (1992). doi:10.1002/jemt.1070210208
84. S.G. Wolf, P. Rez, M. Elbaum, Phosphorus detection in vitrified bacteria by cryo-STEM
annular dark-field analysis. J. Microsc. 260(2), 227–233 (2015). doi:10.1111/jmi.12289
85. S. Asano, B.D. Engel, W. Baumeister, In Situ Cryo-Electron Tomography: A PostReductionist Approach to Structural Biology. J. Mol. Biol. 428(2, Part A), 332–343 (2016).
doi:http://dx.doi.org/10.1016/j.jmb.2015.09.030
86. R. Fernández-Busnadiego, Supramolecular architecture of endoplasmic reticulum–plasma
membrane contact sites. Biochem. Soc. Trans. 44(2), 534–540 (2016). doi:10.1042/
bst20150279
87. R.N. Irobalieva, B. Martins, O. Medalia, Cellular structural biology as revealed by
cryo-electron tomography. J. Cell Sci. 129(3), 469–476 (2016). doi:10.1242/jcs.171967
88. C. Bouchet-Marquis, A. Hoenger, Cryo-electron tomography on vitrified sections: a critical
analysis of benefits and limitations for structural cell biology. Micron (Oxford, England:
1993) 42(2), 152–162 (2011). doi:http://dx.doi.org/10.1016/j.micron.2010.07.003
89. A. Al-Amoudi, A.S. Frangakis, in Three-Dimensional Visualization of the Molecular
Architecture of Cell–Cell Junctions In Situ by Cryo-Electron Tomography of Vitreous
Sections, ed. by C. Has, C. Sitaru. Molecular Dermatology: Methods and Protocols. Humana
Press, Totowa, NJ, pp. 97–117 (2013). doi:10.1007/978-1-62703-227-8_4
90. L. Norlén, O. Öktem, U. Skoglund, Molecular cryo-electron tomography of vitreous tissue
sections: current challenges. J. Microsc. 235(3), 293–307 (2009). doi:10.1111/j.1365-2818.
2009.03219.x
91. T. Wagenknecht, C. Hsieh, M. Marko, Skeletal Muscle Triad Junction Ultrastructure by
Focused-Ion-Beam Milling of Muscle and Cryo-Electron Tomography. European journal of
translational myology 25(1), 4823 (2015). doi:10.4081/ejtm.2015.4823
92. J. Arnold, J. Mahamid, V. Lucic, A. de Marco, J.J. Fernandez, T. Laugks, T. Mayer, A.A.
Hyman, W. Baumeister, J.M. Plitzko, Site-Specific Cryo-focused ion beam sample
preparation guided by 3D correlative microscopy. Biophys. J. 110(4), 860–869 (2016).
doi:10.1016/j.bpj.2015.10.053
93. J. Mahamid, S. Pfeffer, M. Schaffer, E. Villa, R. Danev, L. Kuhn Cuellar, F. Förster, A.A.
Hyman, J.M. Plitzko, W. Baumeister, Visualizing the molecular sociology at the HeLa cell
nuclear periphery. Science 351(6276), 969–972 (2016). doi:10.1126/science.aad8857
2 STEM Tomography in Biology
59
Enzymol. 481, 371–388 (2010). doi:10.1016/S0076-6879(10)81015-8
76. J.P. Buban, Q. Ramasse, B. Gipson, N.D. Browning, H. Stahlberg, High-resolution low-dose
scanning transmission electron microscopy. J. Electron. Microsc. (Tokyo) 59(2), 103–112
(2010). doi:10.1093/jmicro/dfp052
77. R.C. Guerrero-Ferreira, E.R. Wright, Cryo-electron tomography of bacterial viruses.
Virology 435(1), 179–186 (2013). doi:http://dx.doi.org/10.1016/j.virol.2012.08.022
78. K. Celler, R.I. Koning, A.J. Koster, G.P. van Wezel, Multidimensional view of the bacterial
cytoskeleton. J. Bacteriol. 195(8), 1627–1636 (2013). doi:10.1128/jb.02194-12
79. C.M. Oikonomou, G.J. Jensen, A new view into prokaryotic cell biology from electron
cryotomography. Nat. Rev. Micro. 14(4), 205–220 (2016). doi:10.1038/nrmicro.2016.7
80. V. Gold, M. Kudryashev, Recent progress in structure and dynamics of
dual-membrane-spanning bacterial nanomachines. Curr. Opin. Struct. Biol. 39, 1–7
(2016). doi:http://dx.doi.org/10.1016/j.sbi.2016.03.001
81. M.M. Farley, B. Hu, W. Margolin, J. Liu, Minicells, back in fashion. J. Bacteriol. 198(8),
1186–1195 (2016). doi:10.1128/jb.00901-15
82. X. Fu, B.A. Himes, D. Ke, W.J. Rice, J. Ning, P. Zhang, Controlled bacterial lysis for
electron tomography of native cell membranes. Structure 22(12), 1875–1882 (2014). doi:
http://dx.doi.org/10.1016/j.str.2014.09.017
83. P. Rez, W. Chiu, J.K. Weiss, J. Brink, The thickness determination of organic crystals under
low dose conditions using electron energy loss spectroscopy. Microsc. Res. Tech. 21(2),
166–170 (1992). doi:10.1002/jemt.1070210208
84. S.G. Wolf, P. Rez, M. Elbaum, Phosphorus detection in vitrified bacteria by cryo-STEM
annular dark-field analysis. J. Microsc. 260(2), 227–233 (2015). doi:10.1111/jmi.12289
85. S. Asano, B.D. Engel, W. Baumeister, In Situ Cryo-Electron Tomography: A PostReductionist Approach to Structural Biology. J. Mol. Biol. 428(2, Part A), 332–343 (2016).
doi:http://dx.doi.org/10.1016/j.jmb.2015.09.030
86. R. Fernández-Busnadiego, Supramolecular architecture of endoplasmic reticulum–plasma
membrane contact sites. Biochem. Soc. Trans. 44(2), 534–540 (2016). doi:10.1042/
bst20150279
87. R.N. Irobalieva, B. Martins, O. Medalia, Cellular structural biology as revealed by
cryo-electron tomography. J. Cell Sci. 129(3), 469–476 (2016). doi:10.1242/jcs.171967
88. C. Bouchet-Marquis, A. Hoenger, Cryo-electron tomography on vitrified sections: a critical
analysis of benefits and limitations for structural cell biology. Micron (Oxford, England:
1993) 42(2), 152–162 (2011). doi:http://dx.doi.org/10.1016/j.micron.2010.07.003
89. A. Al-Amoudi, A.S. Frangakis, in Three-Dimensional Visualization of the Molecular
Architecture of Cell–Cell Junctions In Situ by Cryo-Electron Tomography of Vitreous
Sections, ed. by C. Has, C. Sitaru. Molecular Dermatology: Methods and Protocols. Humana
Press, Totowa, NJ, pp. 97–117 (2013). doi:10.1007/978-1-62703-227-8_4
90. L. Norlén, O. Öktem, U. Skoglund, Molecular cryo-electron tomography of vitreous tissue
sections: current challenges. J. Microsc. 235(3), 293–307 (2009). doi:10.1111/j.1365-2818.
2009.03219.x
91. T. Wagenknecht, C. Hsieh, M. Marko, Skeletal Muscle Triad Junction Ultrastructure by
Focused-Ion-Beam Milling of Muscle and Cryo-Electron Tomography. European journal of
translational myology 25(1), 4823 (2015). doi:10.4081/ejtm.2015.4823
92. J. Arnold, J. Mahamid, V. Lucic, A. de Marco, J.J. Fernandez, T. Laugks, T. Mayer, A.A.
Hyman, W. Baumeister, J.M. Plitzko, Site-Specific Cryo-focused ion beam sample
preparation guided by 3D correlative microscopy. Biophys. J. 110(4), 860–869 (2016).
doi:10.1016/j.bpj.2015.10.053
93. J. Mahamid, S. Pfeffer, M. Schaffer, E. Villa, R. Danev, L. Kuhn Cuellar, F. Förster, A.A.
Hyman, J.M. Plitzko, W. Baumeister, Visualizing the molecular sociology at the HeLa cell
nuclear periphery. Science 351(6276), 969–972 (2016). doi:10.1126/science.aad8857
2 STEM Tomography in Biology
59