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Volumn 955, Issue , 2013, Pages 171-194

Image processing of 2D crystal images

Author keywords

3D structure determination; Electron crystallography; Electron microscopy; Image processing; Membrane proteins

Indexed keywords

ALGORITHM; CALCULATION; CRYSTAL; CRYSTAL STRUCTURE; FOURIER TRANSFORMATION; IMAGE ANALYSIS; IMAGE PROCESSING; TWO-DIMENSIONAL IMAGING; ARTICLE; CHEMISTRY; COMPUTER PROGRAM; CRYSTALLOGRAPHY; FOURIER ANALYSIS; METHODOLOGY;

EID: 84876041117     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-176-9_10     Document Type: Chapter
Times cited : (10)

References (38)
  • 1
    • 0016842810 scopus 로고
    • Threedimensional model of purple membrane obtained by electron microscopy
    • Henderson R, Unwin PN (1975) Threedimensional model of purple membrane obtained by electron microscopy. Nature 257:28–32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 2
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin PN, Henderson R (1975) Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 94:425–440
    • (1975) J Mol Biol , vol.94 , pp. 425-440
    • Unwin, P.N.1    Henderson, R.2
  • 3
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos LA, Henderson R, Unwin PN (1982) Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Prog Biophys Mol Biol 39:183–231
    • (1982) Prog Biophys Mol Biol , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.3
  • 4
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • Henderson R, Baldwin JM, Downing KH, Lepault J, Zemlin F (1986) Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 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
  • 5
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 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
  • 7
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W, Wang DN, Fujiyoshi Y (1994) Atomic model of plant light-harvesting complex by electron crystallography. Nature 367: 614–621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 9
    • 0035852730 scopus 로고    scopus 로고
    • Visualization of a water-selective pore by electron crystallography in vitreous ice
    • Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK (2001) Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc Natl Acad Sci USA 98:1398–1403
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1398-1403
    • Ren, G.1    Reddy, V.S.2    Cheng, A.3    Melnyk, P.4    Mitra, A.K.5
  • 10
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A, Fujiyoshi Y, Unwin N (2003) Structure and gating mechanism of the acetylcholine receptor pore. Nature 424:949–955
    • (2003) Nature , vol.424 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 11
    • 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 (2004) Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 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
  • 16
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH (1998) Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391:199–203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 17
    • 0032815040 scopus 로고    scopus 로고
    • Ximdisp – a visualization tool to aid structure determination from electron microscope images
    • Smith JM (1999) Ximdisp – a visualization tool to aid structure determination from electron microscope images. J Struct Biol 125: 223–228
    • (1999) J Struct Biol , vol.125 , pp. 223-228
    • Smith, J.M.1
  • 18
    • 0027554794 scopus 로고
    • SPECTRA: A system for processing electron images of crystals
    • Schmid MF, Dargahi R, Tam MW (1993) SPECTRA: a system for processing electron images of crystals. Ultramicroscopy 48: 251–264
    • (1993) Ultramicroscopy , vol.48 , pp. 251-264
    • Schmid, M.F.1    Dargahi, R.2    Tam, M.W.3
  • 19
    • 0029898061 scopus 로고    scopus 로고
    • A brief description of I.C.E.: The integrated crystallographic environment
    • Hardt S, Wang B, Schmid MF (1996) A brief description of I.C.E.: the integrated crystallographic environment. J Struct Biol 116:68–70
    • (1996) J Struct Biol , vol.116 , pp. 68-70
    • Hardt, S.1    Wang, B.2    Schmid, M.F.3
  • 21
    • 0344552378 scopus 로고    scopus 로고
    • Iplt – image processing library and toolkit for the electron microscopy community
    • Philippsen A, Schenk AD, Stahlberg H, Engel A (2003) Iplt – image processing library and toolkit for the electron microscopy community. J Struct Biol 144:4–12
    • (2003) J Struct Biol , vol.144 , pp. 4-12
    • Philippsen, A.1    Schenk, A.D.2    Stahlberg, H.3    Engel, A.4
  • 24
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, Ladjadj M, Leith A (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116:190–199
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 25
    • 0035783171 scopus 로고    scopus 로고
    • Bsoft: Image and molecular processing in electron microscopy
    • Heymann JB (2001) Bsoft: image and molecular processing in electron microscopy. J Struct Biol 133:156–169
    • (2001) J Struct Biol , vol.133 , pp. 156-169
    • Heymann, J.B.1
  • 26
    • 33845330614 scopus 로고    scopus 로고
    • Stahlberg H (2007) 2dx – user-friendly image processing for 2D crystals
    • Gipson B, Zeng X, Zhang Z, Stahlberg H (2007) 2dx – user-friendly image processing for 2D crystals. J Struct Biol 157:64–72
    • J Struct Biol , vol.157 , pp. 64-72
    • Gipson, B.1    Zeng, X.2    Zhang, Z.3
  • 27
    • 36049000626 scopus 로고    scopus 로고
    • Stahlberg H (2007) 2dx_ merge: Data management and merging for 2D crystal images
    • Gipson B, Zeng X, Stahlberg H (2007) 2dx_ merge: data management and merging for 2D crystal images. J Struct Biol 160:375–384
    • J Struct Biol , vol.160 , pp. 375-384
    • Gipson, B.1    Zeng, X.2
  • 28
    • 0002170585 scopus 로고
    • The theoretical resolution limit of the electron microscope
    • Scherzer O (1948) The theoretical resolution limit of the electron microscope. J Appl Phys 20:20–29
    • (1948) J Appl Phys , vol.20 , pp. 20-29
    • Scherzer, O.1
  • 29
    • 0021034131 scopus 로고
    • The importance of beam alignment and crystal tilt in high-resolution electron microscopy
    • Smith DJ, Saxton WO, O’Keefe MA, Wood GJ, Stobbs WM (1983) The importance of beam alignment and crystal tilt in high-resolution electron microscopy. Ultramicroscopy 11: 263–281
    • (1983) Ultramicroscopy , vol.11 , pp. 263-281
    • Smith, D.J.1    Saxton, W.O.2    O’Keefe, M.A.3    Wood, G.J.4    Stobbs, W.M.5
  • 31
    • 79952438103 scopus 로고    scopus 로고
    • Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM
    • Glaeser RM, Typke D, Tiemeijer PC, Pulokas J, Cheng A (2011) Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM. J Struct Biol 174: 1–10
    • (2011) J Struct Biol , vol.174 , pp. 1-10
    • Glaeser, R.M.1    Typke, D.2    Tiemeijer, P.C.3    Pulokas, J.4    Cheng, A.5
  • 33
    • 33845639652 scopus 로고    scopus 로고
    • The contrast-imaging function for tilted specimens
    • Philippsen A, Engel HA, Engel A (2007) The contrast-imaging function for tilted specimens. Ultramicroscopy 107:202–212
    • (2007) Ultramicroscopy , vol.107 , pp. 202-212
    • Philippsen, A.1    Engel, H.A.2    Engel, A.3
  • 34
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142: 334–347
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 35
    • 36048969226 scopus 로고    scopus 로고
    • Automatic lattice determination for two-dimensional crystal images
    • Zeng X, Gipson B, Zheng ZY, Renault L, Stahlberg H (2007) Automatic lattice determination for two-dimensional crystal images. J Struct Biol 160:353–361
    • (2007) J Struct Biol , vol.160 , pp. 353-361
    • Zeng, X.1    Gipson, B.2    Zheng, Z.Y.3    Renault, L.4    Stahlberg, H.5
  • 36
    • 0034712851 scopus 로고    scopus 로고
    • The three-dimensional structure of halorhodopsin to 5 Å by electron crystallography: A new unbending procedure for two-dimensional crystals by using a globalreference structure
    • Kunji ER, von Gronau S, Oesterhelt D, Henderson R (2000) The three-dimensional structure of halorhodopsin to 5 Å by electron crystallography: a new unbending procedure for two-dimensional crystals by using a global reference structure. Proc Natl Acad Sci USA 97:4637–4642
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4637-4642
    • Kunji, E.R.1    Von Gronau, S.2    Oesterhelt, D.3    Henderson, R.4
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs forprotein crystallography
    • Collaborative Computational Project, Number4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760–763
    • (1994) Acta Crystallogr Dbiol Crystallogr , vol.50 , pp. 760-763
  • 38
    • 34548425430 scopus 로고    scopus 로고
    • Amaximum-likelihood approach to two-dimensionalcrystals
    • Zeng X, Stahlberg H, Grigorieff N (2007) A maximum-likelihood approach to two-dimensional crystals. J Struct Biol 160:362–374
    • (2007) J Struct Biol , vol.160 , pp. 362-374
    • Zeng, X.1    Stahlberg, H.2    Grigorieff, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.