12. Adrian M, Dubochet J, Lepault J, McDowall
AW (1984) Cryo-electron microscopy of
viruses. Nature 308:32–36. https://doi.org/
10.1038/308032a0
13. Grimm R, Singh H, Rachel R et al (1998)
Electron tomography of ice-embedded prokaryotic cells. Biophys J 74:1031–1042.
https://doi.org/10.1016/S0006-3495(98)
74028-7
14. Luc ˇic ´ V, Rigort A, Baumeister W (2013) Cryoelectron tomography: the challenge of doing
structural biology in situ. J Cell Biol
202:407–419. https://doi.org/10.1083/jcb.
201304193
15. Serwas D, Su TY, Roessler M et al (2017)
Centrioles initiate cilia assembly but are dispensable for maturation and maintenance in
C. elegans. J Cell Biol 216:1659–1671.
https://doi.org/10.1083/jcb.201610070
16. Moor H (1987) In: Steinbrecht RA, Zierold K
(eds) Theory and practice of high pressure
freezing BT-cryotechniques in biological electron microscopy. Springer, Berlin, Heidelberg,
pp 175–191
17. Frank J (2006) Electron tomography-methods
for three-dimensional visualization of structures in the cell. Springer-Verlag, New York
18. Lin J, Nicastro D (2018) Asymmetric distribution and spatial switching of dynein activity
generates ciliary motility. Science 360:
eaar1968. https://doi.org/10.1126/science.
aar1968
19. Guichard P, Chretien D, Marco S, Tassin AM
(2010) Procentriole assembly revealed by cryoelectron
tomography.
EMBO
J
29:1565–1572.
https://doi.org/10.1038/
emboj.2010.45
20. Danev R, Buijsse B, Khoshouei M et al (2014)
Volta potential phase plate for in-focus phase
contrast transmission electron microscopy.
Proc Natl Acad Sci U S A 111:15635–15640.
https://doi.org/10.1073/pnas.1418377111
21. von Loeffelholz O, Papai G, Danev R et al
(2018) Volta phase plate data collection facilitates image processing and cryo-EM structure
determination. J Struct Biol 202:191–199.
https://doi.org/10.1016/j.jsb.2018.01.003
22. Glaeser RM (2008) Retrospective: radiation
damage and its associated “information limitations”. J Struct Biol 163:271–276. https://
doi.org/10.1016/j.jsb.2008.06.001
23. Talmon Y (1987) In: Steinbrecht RA, Zierold
K (eds) Electron beam radiation damage to
organic
and
biological
cryospecimens
BT-cryotechniques in biological electron
microscopy. Springer, Berlin, Heidelberg, pp
64–84
24. Dierksen K, Typke D, Hegerl R et al (1992)
Towards automatic electron tomography.
Ultramicroscopy 40:71–87. https://doi.org/
10.1016/0304-3991(92)90235-C
25. Koster AJ, Chen H, Sedat JW, Agard DA
(1992) Automated microscopy for electron
tomography. Ultramicroscopy 46:207–227.
https://doi.org/10.1016/0304-3991(92)
90016-D
26. Baumeister W, Grimm R, Walz J (1999) Electron tomography of molecules and cells.
Trends Cell Biol 9:81–85
27. Xiong Q, Morphew MK, Schwartz CL et al
(2009) CTF determination and correction for
low dose tomographic tilt series. J Struct Biol
168:378–387.
https://doi.org/10.1016/j.
jsb.2009.08.016
28. Ferna ´ndez JJ, Li S, Crowther RA (2006) CTF
determination and correction in electron cryotomography. Ultramicroscopy 106:587–596.
https://doi.org/10.1016/j.ultramic.2006.02.
004
29. Turon ˇova ´ B, Schur FKM, Wan W, Briggs JAG
(2017) Efficient 3D-CTF correction for cryoelectron
tomography
using
NovaCTF
improves subtomogram averaging resolution
to 3.4A ˚ . J Struct Biol 199:187–195. https://
doi.org/10.1016/j.jsb.2017.07.007
30. Henderson R, Baldwin JM, Ceska TA et al
(1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J Mol Biol 213:899–929. https://
doi.org/10.1016/S0022-2836(05)80271-2
31. Fernandez J-J, Li S, Bharat TAM, Agard DA
(2018) Cryo-tomography tilt-series alignment
with consideration of the beam-induced sample motion. J Struct Biol 202:200–209.
https://doi.org/10.1016/j.jsb.2018.02.001
32. Hagen WJH, Wan W, Briggs JAG (2017)
Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution
subtomogram averaging. J Struct Biol
197:191–198.
https://doi.org/10.1016/j.
jsb.2016.06.007
33. Grimm R, Koster AJ, Ziese U et al (1996)
Zero-loss energy filtering under low-dose conditions using a post-column energy filter. J
Microsc 183:60–68. https://doi.org/10.
1046/j.1365-2818.1996.77441.x
34. Langmore JP, Smith MF (1992) Quantitative
energy-filtered electron microscopy of
biological molecules in ice. Ultramicroscopy
46:349–373.
https://doi.org/10.1016/
0304-3991(92)90024-E
35. Schro ¨der RR, Hofmann W, Me ´ne ´tret J-F
(1990) Zero-loss energy filtering as improved
imaging mode in cryoelectronmicroscopy of
22
Daniel Serwas and Karen M. Davies
AW (1984) Cryo-electron microscopy of
viruses. Nature 308:32–36. https://doi.org/
10.1038/308032a0
13. Grimm R, Singh H, Rachel R et al (1998)
Electron tomography of ice-embedded prokaryotic cells. Biophys J 74:1031–1042.
https://doi.org/10.1016/S0006-3495(98)
74028-7
14. Luc ˇic ´ V, Rigort A, Baumeister W (2013) Cryoelectron tomography: the challenge of doing
structural biology in situ. J Cell Biol
202:407–419. https://doi.org/10.1083/jcb.
201304193
15. Serwas D, Su TY, Roessler M et al (2017)
Centrioles initiate cilia assembly but are dispensable for maturation and maintenance in
C. elegans. J Cell Biol 216:1659–1671.
https://doi.org/10.1083/jcb.201610070
16. Moor H (1987) In: Steinbrecht RA, Zierold K
(eds) Theory and practice of high pressure
freezing BT-cryotechniques in biological electron microscopy. Springer, Berlin, Heidelberg,
pp 175–191
17. Frank J (2006) Electron tomography-methods
for three-dimensional visualization of structures in the cell. Springer-Verlag, New York
18. Lin J, Nicastro D (2018) Asymmetric distribution and spatial switching of dynein activity
generates ciliary motility. Science 360:
eaar1968. https://doi.org/10.1126/science.
aar1968
19. Guichard P, Chretien D, Marco S, Tassin AM
(2010) Procentriole assembly revealed by cryoelectron
tomography.
EMBO
J
29:1565–1572.
https://doi.org/10.1038/
emboj.2010.45
20. Danev R, Buijsse B, Khoshouei M et al (2014)
Volta potential phase plate for in-focus phase
contrast transmission electron microscopy.
Proc Natl Acad Sci U S A 111:15635–15640.
https://doi.org/10.1073/pnas.1418377111
21. von Loeffelholz O, Papai G, Danev R et al
(2018) Volta phase plate data collection facilitates image processing and cryo-EM structure
determination. J Struct Biol 202:191–199.
https://doi.org/10.1016/j.jsb.2018.01.003
22. Glaeser RM (2008) Retrospective: radiation
damage and its associated “information limitations”. J Struct Biol 163:271–276. https://
doi.org/10.1016/j.jsb.2008.06.001
23. Talmon Y (1987) In: Steinbrecht RA, Zierold
K (eds) Electron beam radiation damage to
organic
and
biological
cryospecimens
BT-cryotechniques in biological electron
microscopy. Springer, Berlin, Heidelberg, pp
64–84
24. Dierksen K, Typke D, Hegerl R et al (1992)
Towards automatic electron tomography.
Ultramicroscopy 40:71–87. https://doi.org/
10.1016/0304-3991(92)90235-C
25. Koster AJ, Chen H, Sedat JW, Agard DA
(1992) Automated microscopy for electron
tomography. Ultramicroscopy 46:207–227.
https://doi.org/10.1016/0304-3991(92)
90016-D
26. Baumeister W, Grimm R, Walz J (1999) Electron tomography of molecules and cells.
Trends Cell Biol 9:81–85
27. Xiong Q, Morphew MK, Schwartz CL et al
(2009) CTF determination and correction for
low dose tomographic tilt series. J Struct Biol
168:378–387.
https://doi.org/10.1016/j.
jsb.2009.08.016
28. Ferna ´ndez JJ, Li S, Crowther RA (2006) CTF
determination and correction in electron cryotomography. Ultramicroscopy 106:587–596.
https://doi.org/10.1016/j.ultramic.2006.02.
004
29. Turon ˇova ´ B, Schur FKM, Wan W, Briggs JAG
(2017) Efficient 3D-CTF correction for cryoelectron
tomography
using
NovaCTF
improves subtomogram averaging resolution
to 3.4A ˚ . J Struct Biol 199:187–195. https://
doi.org/10.1016/j.jsb.2017.07.007
30. Henderson R, Baldwin JM, Ceska TA et al
(1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J Mol Biol 213:899–929. https://
doi.org/10.1016/S0022-2836(05)80271-2
31. Fernandez J-J, Li S, Bharat TAM, Agard DA
(2018) Cryo-tomography tilt-series alignment
with consideration of the beam-induced sample motion. J Struct Biol 202:200–209.
https://doi.org/10.1016/j.jsb.2018.02.001
32. Hagen WJH, Wan W, Briggs JAG (2017)
Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution
subtomogram averaging. J Struct Biol
197:191–198.
https://doi.org/10.1016/j.
jsb.2016.06.007
33. Grimm R, Koster AJ, Ziese U et al (1996)
Zero-loss energy filtering under low-dose conditions using a post-column energy filter. J
Microsc 183:60–68. https://doi.org/10.
1046/j.1365-2818.1996.77441.x
34. Langmore JP, Smith MF (1992) Quantitative
energy-filtered electron microscopy of
biological molecules in ice. Ultramicroscopy
46:349–373.
https://doi.org/10.1016/
0304-3991(92)90024-E
35. Schro ¨der RR, Hofmann W, Me ´ne ´tret J-F
(1990) Zero-loss energy filtering as improved
imaging mode in cryoelectronmicroscopy of
22
Daniel Serwas and Karen M. Davies