crystallography: application to structural study
on bacteriorhodopsin. J Electron Microsc 48
(5):653–658
37. Henderson R, Unwin PN (1975) Threedimensional model of purple membrane
obtained by electron microscopy. Nature 257
(5521):28–32
38. Russo CJ, Henderson R (2018) Charge accumulation in electron cryomicroscopy. Ultramicroscopy 187:43–49
39. Gyobu N et al (2004) Improved specimen
preparation for cryo-electron microscopy
using a symmetric carbon sandwich technique.
J Struct Biol 146(3):325–333
40. Bullough P, Henderson R (1987) Use of spotscan procedure for recording low-dose micrographs of beam-sensitive specimens. Ultramicroscopy 21(3):223–230
41. Downing KH, Glaeser RM (1986) Improvement in high resolution image quality of
radiation-sensitive specimens achieved with
reduced spot size of the electron beam. Ultramicroscopy 20(3):269–278
42. Grant T, Grigorieff N (2015) Measuring the
optimal exposure for single particle cryo-EM
using a 2.6 A ˚ reconstruction of rotavirus VP6.
elife 4:e06980
43. Schenk AD et al (2013) A pipeline for comprehensive and automated processing of electron
diffraction data in IPLT. J Struct Biol 182
(2):173–185
44. Gipson B et al (2007) 2dx_merge: data management and merging for 2D crystal images. J
Struct Biol 160(3):375–384
45. Gipson B et al (2007) 2dx--user-friendly image
processing for 2D crystals. J Struct Biol 157
(1):64–72
46. Wall J et al (1985) Films that wet without glow
discharge, 35th EMSA meeting. San Francisco
Press, Louisville
47. Kittel C, McEuen P (1996) Introduction to
solid state physics. Wiley, New York
48. Perkins GA et al (1993) Glucose alone does not
completely hydrate bacteriorhodopsin in
glucose-embedded purple membrane. J
Microsc 169(Pt 1):61–65
49. Kimura Y et al (1997) Surface of bacteriorhodopsin revealed by high-resolution electron
crystallography. Nature 389(6647):206–211
50. Booy FP, Pawley JB (1993) Cryo-crinkling:
what happens to carbon films on copper grids
at low temperature. Ultramicroscopy 48
(3):273–280
Electron Crystallography of Membrane Proteins
265
on bacteriorhodopsin. J Electron Microsc 48
(5):653–658
37. Henderson R, Unwin PN (1975) Threedimensional model of purple membrane
obtained by electron microscopy. Nature 257
(5521):28–32
38. Russo CJ, Henderson R (2018) Charge accumulation in electron cryomicroscopy. Ultramicroscopy 187:43–49
39. Gyobu N et al (2004) Improved specimen
preparation for cryo-electron microscopy
using a symmetric carbon sandwich technique.
J Struct Biol 146(3):325–333
40. Bullough P, Henderson R (1987) Use of spotscan procedure for recording low-dose micrographs of beam-sensitive specimens. Ultramicroscopy 21(3):223–230
41. Downing KH, Glaeser RM (1986) Improvement in high resolution image quality of
radiation-sensitive specimens achieved with
reduced spot size of the electron beam. Ultramicroscopy 20(3):269–278
42. Grant T, Grigorieff N (2015) Measuring the
optimal exposure for single particle cryo-EM
using a 2.6 A ˚ reconstruction of rotavirus VP6.
elife 4:e06980
43. Schenk AD et al (2013) A pipeline for comprehensive and automated processing of electron
diffraction data in IPLT. J Struct Biol 182
(2):173–185
44. Gipson B et al (2007) 2dx_merge: data management and merging for 2D crystal images. J
Struct Biol 160(3):375–384
45. Gipson B et al (2007) 2dx--user-friendly image
processing for 2D crystals. J Struct Biol 157
(1):64–72
46. Wall J et al (1985) Films that wet without glow
discharge, 35th EMSA meeting. San Francisco
Press, Louisville
47. Kittel C, McEuen P (1996) Introduction to
solid state physics. Wiley, New York
48. Perkins GA et al (1993) Glucose alone does not
completely hydrate bacteriorhodopsin in
glucose-embedded purple membrane. J
Microsc 169(Pt 1):61–65
49. Kimura Y et al (1997) Surface of bacteriorhodopsin revealed by high-resolution electron
crystallography. Nature 389(6647):206–211
50. Booy FP, Pawley JB (1993) Cryo-crinkling:
what happens to carbon films on copper grids
at low temperature. Ultramicroscopy 48
(3):273–280
Electron Crystallography of Membrane Proteins
265
