메뉴 건너뛰기




Volumn 42, Issue 2, 2011, Pages 132-140

Specimen preparation for electron diffraction of thin crystals

Author keywords

Diffraction; Electron crystallography; Protein structure; Specimen preparation

Indexed keywords

ATOMIC RESOLUTION; DATA COLLECTION PROTOCOLS; DEGREE OF ORDER; DIFFRACTION SPOTS; ELECTRON CRYSTALLOGRAPHIC DATA; ELECTRON CRYSTALLOGRAPHY; ELECTRON DIFFRACTION DATA; HIGH RESOLUTION; HIGH TILT ANGLE; NATIVE STATE; ORGANIC MOLECULES; PROTEIN CRYSTAL; PROTEIN STRUCTURE; PROTEIN STRUCTURES; SPECIMEN PREPARATION METHOD; STRUCTURAL CHARACTERIZATION; STRUCTURAL INFORMATION; THIN CRYSTAL;

EID: 78649807389     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2010.05.003     Document Type: Review
Times cited : (5)

References (49)
  • 1
    • 0021095146 scopus 로고
    • Equivalence of the projected structure of thin catalase crystals preserved for electron microscopy by negative stain, glucose or embedding in the presence of tannic acid
    • Akey C.W., Edelstein S.J. Equivalence of the projected structure of thin catalase crystals preserved for electron microscopy by negative stain, glucose or embedding in the presence of tannic acid. J. Mol. Biol. 1983, 163:575-612.
    • (1983) J. Mol. Biol. , vol.163 , pp. 575-612
    • Akey, C.W.1    Edelstein, S.J.2
  • 2
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos L.A., Henderson R., Unwin P.N.T. Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Prog. Biophys. Mol. Biol. 1982, 39:183-231.
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.T.3
  • 3
    • 0027561407 scopus 로고
    • Cryo-crinkling: what happens to carbon films on copper grids at low temperature
    • Booy F.P., Pawley J.B. Cryo-crinkling: what happens to carbon films on copper grids at low temperature. Ultramicroscopy 1993, 48:273-280.
    • (1993) Ultramicroscopy , vol.48 , pp. 273-280
    • Booy, F.P.1    Pawley, J.B.2
  • 4
    • 0026499357 scopus 로고
    • Has negative staining still a place in biomacromolecular electron-microscopy
    • Bremer A., Henn C., Engel A., Baumeister W., Aebi U. Has negative staining still a place in biomacromolecular electron-microscopy. Ultramicroscopy 1992, 46:85-111.
    • (1992) Ultramicroscopy , vol.46 , pp. 85-111
    • Bremer, A.1    Henn, C.2    Engel, A.3    Baumeister, W.4    Aebi, U.5
  • 5
    • 0026230169 scopus 로고
    • Effect of surface-roughness of carbon support films on high-resolution electron-diffraction of 2-dimensional protein crystals
    • Butt H.J., Wang D.N., Hansma P.K., Kühlbrandt W. Effect of surface-roughness of carbon support films on high-resolution electron-diffraction of 2-dimensional protein crystals. Ultramicroscopy 1991, 36:307-318.
    • (1991) Ultramicroscopy , vol.36 , pp. 307-318
    • Butt, H.J.1    Wang, D.N.2    Hansma, P.K.3    Kühlbrandt, W.4
  • 6
    • 0025312416 scopus 로고
    • Analysis of high-resolution electron diffraction patterns from purple membrane labelled with heavy-atoms
    • Ceska T.A., Henderson R. Analysis of high-resolution electron diffraction patterns from purple membrane labelled with heavy-atoms. J. Mol. Biol. 1990, 213:539-560.
    • (1990) J. Mol. Biol. , vol.213 , pp. 539-560
    • Ceska, T.A.1    Henderson, R.2
  • 7
    • 36049014442 scopus 로고    scopus 로고
    • Towards automated screening of two-dimensional crystals
    • Cheng A., et al. Towards automated screening of two-dimensional crystals. J. Struct. Biol. 2007, 160:324-331.
    • (2007) J. Struct. Biol. , vol.160 , pp. 324-331
    • Cheng, A.1
  • 8
    • 0000766925 scopus 로고
    • The scattering of electrons by a single crystal of nickel
    • Davisson C., Germer L.H. The scattering of electrons by a single crystal of nickel. Nature 1927, 119:558-560.
    • (1927) Nature , vol.119 , pp. 558-560
    • Davisson, C.1    Germer, L.H.2
  • 10
    • 0026031904 scopus 로고
    • Spot-scan imaging in transmission electron microscopy
    • Downing K.H. Spot-scan imaging in transmission electron microscopy. Science 1991, 251:53-59.
    • (1991) Science , vol.251 , pp. 53-59
    • Downing, K.H.1
  • 11
    • 0026499524 scopus 로고
    • Automatic focus correction for spot-scan imaging of tilted specimens
    • Downing K.H. Automatic focus correction for spot-scan imaging of tilted specimens. Ultramicroscopy 1992, 46:199-206.
    • (1992) Ultramicroscopy , vol.46 , pp. 199-206
    • Downing, K.H.1
  • 12
    • 0039841987 scopus 로고    scopus 로고
    • Accurate recording and measurement of electron diffraction data in structural and difference Fourier studies of proteins
    • Downing K.H., Li H.L. Accurate recording and measurement of electron diffraction data in structural and difference Fourier studies of proteins. Microsc. Microanal. 2001, 7:407-417.
    • (2001) Microsc. Microanal. , vol.7 , pp. 407-417
    • Downing, K.H.1    Li, H.L.2
  • 13
    • 0020220722 scopus 로고
    • The mounting of macromolecules for electron microscopy with particular reference to surface phenomena and treatment of support films by glow discharge
    • Academic Press, London
    • Dubochet J., Groom M., Mueller-Neuteboom S. The mounting of macromolecules for electron microscopy with particular reference to surface phenomena and treatment of support films by glow discharge. Adv. Opt. Elec. Microsc. 1982, vol. 7. Academic Press, London.
    • (1982) Adv. Opt. Elec. Microsc. , vol.7
    • Dubochet, J.1    Groom, M.2    Mueller-Neuteboom, S.3
  • 14
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi Y. The structural study of membrane proteins by electron crystallography. Adv. Biophys. 1998, 35:25-80.
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 15
    • 53249115170 scopus 로고    scopus 로고
    • Electron crystallography of proteins in membranes
    • Fujiyoshi Y., Unwin N. Electron crystallography of proteins in membranes. Curr. Opin. Struct. Biol. 2008, 18:587-592.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 587-592
    • Fujiyoshi, Y.1    Unwin, N.2
  • 16
    • 0026053859 scopus 로고
    • Interfacial energies and surface-tension forces involved in the preparation of thin, flat crystals of biological macromolecules for high-resolution electron-microscopy
    • Glaeser R.M., Zilker A., Radermacher M., Gaub H.E., Hartmann T., Baumeister W. Interfacial energies and surface-tension forces involved in the preparation of thin, flat crystals of biological macromolecules for high-resolution electron-microscopy. J. Microsc. 1991, 161:21-45.
    • (1991) J. Microsc. , vol.161 , pp. 21-45
    • Glaeser, R.M.1    Zilker, A.2    Radermacher, M.3    Gaub, H.E.4    Hartmann, T.5    Baumeister, W.6
  • 18
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen T., Sliz P., Kistler J., Cheng Y., Walz T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 2004, 429:193-197.
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 19
    • 1942521362 scopus 로고    scopus 로고
    • Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique
    • Gyobu N., Tani K., Hiroaki Y., Kamegawa A., Mitsuoka K., Fujiyoshi Y. Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique. J. Struct. Biol. 2004, 146:325-333.
    • (2004) J. Struct. Biol. , vol.146 , pp. 325-333
    • Gyobu, N.1    Tani, K.2    Hiroaki, Y.3    Kamegawa, A.4    Mitsuoka, K.5    Fujiyoshi, Y.6
  • 20
  • 21
    • 0027144770 scopus 로고
    • Projection structure of halorhodopsin from Halobacterium halobium at 6 A resolution obtained by electron cryo-microscopy
    • Havelka W.A., Henderson R., Heymann J.A., Oesterhelt D. Projection structure of halorhodopsin from Halobacterium halobium at 6 A resolution obtained by electron cryo-microscopy. J. Mol. Biol. 1993, 234:837-846.
    • (1993) J. Mol. Biol. , vol.234 , pp. 837-846
    • Havelka, W.A.1    Henderson, R.2    Heymann, J.A.3    Oesterhelt, D.4
  • 23
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 1990, 213:899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 24
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5Å resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., Zemlin F. Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5Å resolution. Ultramicroscopy 1986, 19:147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 25
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 1975, 257:28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 26
    • 0032695274 scopus 로고    scopus 로고
    • Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin
    • Hirai T., Murata K., Mitsuoka K., Kimura Y., Fujiyoshi Y. Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin. J. Electron. Microsc. (Tokyo) 1999, 48:653-658.
    • (1999) J. Electron. Microsc. (Tokyo) , vol.48 , pp. 653-658
    • Hirai, T.1    Murata, K.2    Mitsuoka, K.3    Kimura, Y.4    Fujiyoshi, Y.5
  • 27
    • 29144521255 scopus 로고    scopus 로고
    • Implications of the aquaporin-4 structure on array formation and cell adhesion
    • Hiroaki Y., et al. Implications of the aquaporin-4 structure on array formation and cell adhesion. J. Mol. Biol. 2006, 355:628-639.
    • (2006) J. Mol. Biol. , vol.355 , pp. 628-639
    • Hiroaki, Y.1
  • 28
    • 33745938162 scopus 로고    scopus 로고
    • Structural basis for detoxification and oxidative stress protection in membranes
    • Holm P.J., et al. Structural basis for detoxification and oxidative stress protection in membranes. J. Mol. Biol. 2006, 360:934-945.
    • (2006) J. Mol. Biol. , vol.360 , pp. 934-945
    • Holm, P.J.1
  • 29
    • 77953600862 scopus 로고    scopus 로고
    • Automated electron microscopy for evaluating two-dimensional crystallization of membrane proteins
    • ePub ahead of print
    • Hu M., et al. Automated electron microscopy for evaluating two-dimensional crystallization of membrane proteins. J. Struct. Biol. 2010, ePub ahead of print.
    • (2010) J. Struct. Biol.
    • Hu, M.1
  • 30
    • 0025297219 scopus 로고
    • Structure of PhoE porin in projection at 3.5Å resolution
    • Jap B.K., Downing K.H., Walian P.J. Structure of PhoE porin in projection at 3.5Å resolution. J. Struct. Biol. 1990, 103:57-63.
    • (1990) J. Struct. Biol. , vol.103 , pp. 57-63
    • Jap, B.K.1    Downing, K.H.2    Walian, P.J.3
  • 32
    • 49649104307 scopus 로고    scopus 로고
    • Structural basis for induced formation of the inflammatory mediator prostaglandin E2
    • Jegerschold C., et al. Structural basis for induced formation of the inflammatory mediator prostaglandin E2. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:11110-11115.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 11110-11115
    • Jegerschold, C.1
  • 34
    • 0024974779 scopus 로고
    • Two-dimensional structure of plant light-harvesting complex at 3.7 A resolution by electron crystallography
    • Kühlbrandt W., Downing K.H. Two-dimensional structure of plant light-harvesting complex at 3.7 A resolution by electron crystallography. J. Mol. Biol. 1989, 207:823-826.
    • (1989) J. Mol. Biol. , vol.207 , pp. 823-826
    • Kühlbrandt, W.1    Downing, K.H.2
  • 35
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D.N., Fujiyoshi Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 1994, 367:614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 36
    • 34248594947 scopus 로고    scopus 로고
    • Automated 100-position specimen loader and image acquisition system for transmission electron microscopy
    • Lefman J., Morrison R., Subramaniam S. Automated 100-position specimen loader and image acquisition system for transmission electron microscopy. J. Struct. Biol. 2007, 158:318-326.
    • (2007) J. Struct. Biol. , vol.158 , pp. 318-326
    • Lefman, J.1    Morrison, R.2    Subramaniam, S.3
  • 37
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Löwe J., Li H., Downing K.H., Nogales E. Refined structure of alpha beta-tubulin at 3.5 A resolution. J. Mol. Biol. 2001, 313:1045-1057.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 38
    • 0034609808 scopus 로고    scopus 로고
    • Structural determinants of water permeation through aquaporin-1
    • Murata K., et al. Structural determinants of water permeation through aquaporin-1. Nature 2000, 407:599-605.
    • (2000) Nature , vol.407 , pp. 599-605
    • Murata, K.1
  • 39
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., Downing K.H. Structure of the alpha beta tubulin dimer by electron crystallography. Nature 1998, 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 40
    • 0028856299 scopus 로고
    • Preservation of 2-D crystals of tubulin for electron crystallography
    • Nogales E., Wolf S.G., Zhang S.X., Downing K.H. Preservation of 2-D crystals of tubulin for electron crystallography. J. Struct. Biol. 1995, 115:199-208.
    • (1995) J. Struct. Biol. , vol.115 , pp. 199-208
    • Nogales, E.1    Wolf, S.G.2    Zhang, S.X.3    Downing, K.H.4
  • 41
    • 67650282016 scopus 로고    scopus 로고
    • Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment
    • Raunser S., Walz T. Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment. Annu. Rev. Biophys. 2009, 38:89-105.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 89-105
    • Raunser, S.1    Walz, T.2
  • 42
    • 0035852730 scopus 로고    scopus 로고
    • Visualization of a water-selective pore by electron crystallography in vitreous ice
    • Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K. Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:1398-1403.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1398-1403
    • Ren, G.1    Reddy, V.S.2    Cheng, A.3    Melnyk, P.4    Mitra, A.K.5
  • 43
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor K.A., Glaeser R.M. Electron diffraction of frozen, hydrated protein crystals. Science 1974, 186:1036-1037.
    • (1974) Science , vol.186 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 44
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin P.N., Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 1975, 94:425-440.
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.1    Henderson, R.2
  • 45
    • 0034333321 scopus 로고    scopus 로고
    • Parameters affecting specimen flatness of two-dimensional crystals for electron crystallography
    • Vonck J. Parameters affecting specimen flatness of two-dimensional crystals for electron crystallography. Ultramicroscopy 2000, 85:123-129.
    • (2000) Ultramicroscopy , vol.85 , pp. 123-129
    • Vonck, J.1
  • 46
    • 0025091681 scopus 로고
    • Three-dimensional electron diffraction of PhoE porin to 2.8 A resolution
    • Walian P.J., Jap B.K. Three-dimensional electron diffraction of PhoE porin to 2.8 A resolution. J. Mol. Biol. 1990, 215:429-438.
    • (1990) J. Mol. Biol. , vol.215 , pp. 429-438
    • Walian, P.J.1    Jap, B.K.2
  • 48
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • Wang D.N., Kühlbrandt W. High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J. Mol. Biol. 1991, 217:691-699.
    • (1991) J. Mol. Biol. , vol.217 , pp. 691-699
    • Wang, D.N.1    Kühlbrandt, W.2
  • 49
    • 0036229990 scopus 로고    scopus 로고
    • Quantitative comparison of zero-loss and conventional electron diffraction from two-dimensional and thin three-dimensional protein crystals
    • Yonekura K., Maki-Yonekura S., Namba K. Quantitative comparison of zero-loss and conventional electron diffraction from two-dimensional and thin three-dimensional protein crystals. Biophys. J. 2002, 82:2784-2797.
    • (2002) Biophys. J. , vol.82 , pp. 2784-2797
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.