9. Hattne J, Shi D, Glynn C, Zee C-T, GallagherJones M, Martynowycz MW et al (2018) Analysis of global and site-specific radiation damage
in cryo-EM. Structure [Internet] 26
(5):759–766.e4. https://linkinghub.elsevier.
com/retrieve/pii/S0969212618301254
10. Hattne J, Martynowycz MW, Penczek PA,
Gonen T (2019) MicroED with the falcon III
direct electron detector. IUCrJ [Internet] 6
(5):921–926. http://scripts.iucr.org/cgi-bin/
paper?S2052252519010583
11. Nederlof I, Li Y-WW, Van Heel M, Abrahams
JP (2013) Imaging protein three-dimensional
nanocrystals with cryo-EM. Acta Crystallogr
Sect D Biol Crystallogr 69(Pt 5):852–859
12. Nave C, Hill MA (2005) Will reduced radiation
damage occur with very small crystals? J Synchrotron Radiat [Internet] 12(Pt 3):299–303.
http://www.ncbi.nlm.nih.gov/pubmed/
15840914
13. Subramanian G, Basu S, Liu H, Zuo J-M,
Spence JCH (2015) Solving protein nanocrystals by cryo-EM diffraction: multiple scattering
artifacts.
Ultramicroscopy
[Internet]
148:87–93. http://linkinghub.elsevier.com/
retrieve/pii/S0304399114001715
14. Nannenga BL, Shi D, Leslie AGWW, Gonen T
(2014) High-resolution structure determination by continuous-rotation data collection in
MicroEDED. Nat Methods [Internet] 11
(9):927–930. http://www.ncbi.nlm.nih.gov/
pubmed/25086503
15. Wang B, Zou X, Smeets S (2019) Automated
serial rotation electron diffraction combined
with cluster analysis: an efficient multi-crystal
workflow for structure determination. IUCrJ 6
(5):1–14
16. Duyvesteyn HME, Kotecha A, Ginn HM,
Hecksel CW, Beale EV, de Haas F et al (2018)
Machining protein microcrystals for structure
determination by electron diffraction. Proc
Natl Acad Sci [Internet] 115(38):9569–9573.
https://doi.org/10.1073/pnas.1809978115
17. Martynowycz MW, Zhao W, Hattne J, Jensen
GJ, Gonen T (2019) Qualitative analyses of
polishing and precoating FIB milled crystals
for MicroED. Structure [Internet] 27
(10):1594–1600.e2.
https://doi.org/10.
1016/j.str.2019.07.004
18. Gevorkov Y, Barty A, Brehm W, White TA,
Tolstikova A, Wiedorn MO et al (2020) PinkIndexer—a universal indexer for pink-beam
X-ray and electron diffraction snapshots. Acta
Crystallogr Sect A Found Adv [Internet] 76
(2):121–131. http://scripts.iucr.org/cgi-bin/
paper?S2053273319015559
19. Hattne J, Reyes FE, Nannenga BL, Shi D, de la
Cruz MJ, Leslie AGWW et al (2015) MicroED
data collection and processing. Acta
Crystallogr Sect A Found Adv [Internet] 71
(4):353–360. http://scripts.iucr.org/cgi-bin/
paper?S2053273315010669
20. Clabbers MTBB, Gruene T, Parkhurst JM,
Abrahams JP, Waterman DG (2018) Electron
diffraction data processing with DIALS. Acta
Crystallogr Sect D Struct Biol [Internet] 74
(6):506–518. http://scripts.iucr.org/cgi-bin/
paper?S2059798318007726
21. Henderson R, Unwin PNT (1975) Threedimensional model of purple membrane
obtained by electron microscopy. Nature
[Internet] 257(5521):28–32. http://www.
nature.com/articles/257028a0
22. Hayward SB, Glaeser RM (1979) Radiation
damage of purple membrane at low temperature.
Ultramicroscopy
[Internet]
4
(2):201–210.
https://linkinghub.elsevier.
com/retrieve/pii/S0304399179902110
23. Uyeda N, Kobayashi T, Ishizuka K, Fujiyoshi Y
(1980) Crystal structure of Ag TCNQ. Nature
[Internet] 285(5760):95–97. http://www.
nature.com/articles/285095b0
24. Jeng T-W, Chiu W (1984) Quantitative assessment of radiation damage in a thin protein
crystal. J Microsc [Internet] 136(1):35–44.
https://doi.org/10.1111/j.1365-2818.1984.
tb02544.x
25. Meents A, Gutmann S, Wagner A, SchulzeBriese C (2010) Origin and temperature
dependence of radiation damage in biological
samples at cryogenic temperatures. Proc Natl
Acad Sci U S A 107(3):1094–1099
26. Glaeser RM (1971) Limitations to significant
information in biological electron microscopy
as a result of radiation damage. J Ultrastruct
Res [Internet] 36(3–4):466–482. https://
linkinghub.elsevier.com/retrieve/pii/
S0022532071801181
27. Paithankar KS, Owen RL, Garman EF (2009)
Absorbed dose calculations for macromolecular crystals: improvements to RADDOSE. J
Synchrotron
Radiat
[Internet]
16
(2):152–162. http://scripts.iucr.org/cgi-bin/
paper?S0909049508040430
28. Zeldin OB, Gerstel M, Garman EF (2013)
RADDOSE-3D: time- and space-resolved
modelling of dose in macromolecular crystallography. J Appl Crystallogr [Internet] 46
(4):1225–1230.
http://gateway.
webofknowledge.com/gateway/Gateway.cgi?
GWVersion¼2&SrcAuth¼mekentosj&
SrcApp¼Papers&Des
tLinkType¼FullRecord&DestApp¼WOS&
KeyUT¼000322032300053
29. Berger MJ, Coursey JS, Zucker MA, Chang J
(2005) Stopping-power & range tables for
electrons, protons, and helium ions [Internet].
http://physics.nist.gov/Star
318
Johan Hattne
in cryo-EM. Structure [Internet] 26
(5):759–766.e4. https://linkinghub.elsevier.
com/retrieve/pii/S0969212618301254
10. Hattne J, Martynowycz MW, Penczek PA,
Gonen T (2019) MicroED with the falcon III
direct electron detector. IUCrJ [Internet] 6
(5):921–926. http://scripts.iucr.org/cgi-bin/
paper?S2052252519010583
11. Nederlof I, Li Y-WW, Van Heel M, Abrahams
JP (2013) Imaging protein three-dimensional
nanocrystals with cryo-EM. Acta Crystallogr
Sect D Biol Crystallogr 69(Pt 5):852–859
12. Nave C, Hill MA (2005) Will reduced radiation
damage occur with very small crystals? J Synchrotron Radiat [Internet] 12(Pt 3):299–303.
http://www.ncbi.nlm.nih.gov/pubmed/
15840914
13. Subramanian G, Basu S, Liu H, Zuo J-M,
Spence JCH (2015) Solving protein nanocrystals by cryo-EM diffraction: multiple scattering
artifacts.
Ultramicroscopy
[Internet]
148:87–93. http://linkinghub.elsevier.com/
retrieve/pii/S0304399114001715
14. Nannenga BL, Shi D, Leslie AGWW, Gonen T
(2014) High-resolution structure determination by continuous-rotation data collection in
MicroEDED. Nat Methods [Internet] 11
(9):927–930. http://www.ncbi.nlm.nih.gov/
pubmed/25086503
15. Wang B, Zou X, Smeets S (2019) Automated
serial rotation electron diffraction combined
with cluster analysis: an efficient multi-crystal
workflow for structure determination. IUCrJ 6
(5):1–14
16. Duyvesteyn HME, Kotecha A, Ginn HM,
Hecksel CW, Beale EV, de Haas F et al (2018)
Machining protein microcrystals for structure
determination by electron diffraction. Proc
Natl Acad Sci [Internet] 115(38):9569–9573.
https://doi.org/10.1073/pnas.1809978115
17. Martynowycz MW, Zhao W, Hattne J, Jensen
GJ, Gonen T (2019) Qualitative analyses of
polishing and precoating FIB milled crystals
for MicroED. Structure [Internet] 27
(10):1594–1600.e2.
https://doi.org/10.
1016/j.str.2019.07.004
18. Gevorkov Y, Barty A, Brehm W, White TA,
Tolstikova A, Wiedorn MO et al (2020) PinkIndexer—a universal indexer for pink-beam
X-ray and electron diffraction snapshots. Acta
Crystallogr Sect A Found Adv [Internet] 76
(2):121–131. http://scripts.iucr.org/cgi-bin/
paper?S2053273319015559
19. Hattne J, Reyes FE, Nannenga BL, Shi D, de la
Cruz MJ, Leslie AGWW et al (2015) MicroED
data collection and processing. Acta
Crystallogr Sect A Found Adv [Internet] 71
(4):353–360. http://scripts.iucr.org/cgi-bin/
paper?S2053273315010669
20. Clabbers MTBB, Gruene T, Parkhurst JM,
Abrahams JP, Waterman DG (2018) Electron
diffraction data processing with DIALS. Acta
Crystallogr Sect D Struct Biol [Internet] 74
(6):506–518. http://scripts.iucr.org/cgi-bin/
paper?S2059798318007726
21. Henderson R, Unwin PNT (1975) Threedimensional model of purple membrane
obtained by electron microscopy. Nature
[Internet] 257(5521):28–32. http://www.
nature.com/articles/257028a0
22. Hayward SB, Glaeser RM (1979) Radiation
damage of purple membrane at low temperature.
Ultramicroscopy
[Internet]
4
(2):201–210.
https://linkinghub.elsevier.
com/retrieve/pii/S0304399179902110
23. Uyeda N, Kobayashi T, Ishizuka K, Fujiyoshi Y
(1980) Crystal structure of Ag TCNQ. Nature
[Internet] 285(5760):95–97. http://www.
nature.com/articles/285095b0
24. Jeng T-W, Chiu W (1984) Quantitative assessment of radiation damage in a thin protein
crystal. J Microsc [Internet] 136(1):35–44.
https://doi.org/10.1111/j.1365-2818.1984.
tb02544.x
25. Meents A, Gutmann S, Wagner A, SchulzeBriese C (2010) Origin and temperature
dependence of radiation damage in biological
samples at cryogenic temperatures. Proc Natl
Acad Sci U S A 107(3):1094–1099
26. Glaeser RM (1971) Limitations to significant
information in biological electron microscopy
as a result of radiation damage. J Ultrastruct
Res [Internet] 36(3–4):466–482. https://
linkinghub.elsevier.com/retrieve/pii/
S0022532071801181
27. Paithankar KS, Owen RL, Garman EF (2009)
Absorbed dose calculations for macromolecular crystals: improvements to RADDOSE. J
Synchrotron
Radiat
[Internet]
16
(2):152–162. http://scripts.iucr.org/cgi-bin/
paper?S0909049508040430
28. Zeldin OB, Gerstel M, Garman EF (2013)
RADDOSE-3D: time- and space-resolved
modelling of dose in macromolecular crystallography. J Appl Crystallogr [Internet] 46
(4):1225–1230.
http://gateway.
webofknowledge.com/gateway/Gateway.cgi?
GWVersion¼2&SrcAuth¼mekentosj&
SrcApp¼Papers&Des
tLinkType¼FullRecord&DestApp¼WOS&
KeyUT¼000322032300053
29. Berger MJ, Coursey JS, Zucker MA, Chang J
(2005) Stopping-power & range tables for
electrons, protons, and helium ions [Internet].
http://physics.nist.gov/Star
318
Johan Hattne