메뉴 건너뛰기




Volumn 160, Issue 3, 2007, Pages 362-374

A maximum likelihood approach to two-dimensional crystals

Author keywords

2dx; Electron crystallography; Maximum likelihood; Protein structure; Single particle

Indexed keywords

PROTEIN;

EID: 34548425430     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.09.013     Document Type: Article
Times cited : (35)

References (38)
  • 1
    • 34548402962 scopus 로고    scopus 로고
    • The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 Å resolution
    • Chiu P.-L., Pagel M., Evans J.E., Chou H.-T., Zeng X., Gipson B., Stahlberg H., and Nimigean C.M. The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 Å resolution. Structure 15 (2007) 1053-1064
    • (2007) Structure , vol.15 , pp. 1053-1064
    • Chiu, P.-L.1    Pagel, M.2    Evans, J.E.3    Chou, H.-T.4    Zeng, X.5    Gipson, B.6    Stahlberg, H.7    Nimigean, C.M.8
  • 3
    • 0002629270 scopus 로고
    • Maximum likelihood from incomplete data via the EM algorithm
    • Dempster A., Laird N., and Rubin D. Maximum likelihood from incomplete data via the EM algorithm. J. R. Stat. Soc. Ser. B (1977) 1-38
    • (1977) J. R. Stat. Soc. Ser. B , pp. 1-38
    • Dempster, A.1    Laird, N.2    Rubin, D.3
  • 4
    • 0000186608 scopus 로고
    • Measurement and compensation of defocussing and aberrations by fourier processing of electron micrographs
    • Erickson H.P., and Klug A. Measurement and compensation of defocussing and aberrations by fourier processing of electron micrographs. Phil. Trans. R. Soc. 261B (1971) 105-118
    • (1971) Phil. Trans. R. Soc. , vol.261 B , pp. 105-118
    • Erickson, H.P.1    Klug, A.2
  • 7
    • 36048986445 scopus 로고    scopus 로고
    • Gipson, B., Zeng, X., Wouts, R., Kühlbrandt, W., Stahlberg, H., this issue. 2dx_merge-User-friendly merging for 2D crystals. J. Struct. Biol.
  • 8
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • Grigorieff N. Resolution measurement in structures derived from single particles. Acta Crystallogr. D Biol. Crystallogr. 56 Pt. 10 (2000) 1270-1277
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , Issue.PART 10 , pp. 1270-1277
    • Grigorieff, N.1
  • 9
    • 0029620939 scopus 로고
    • Lipid location in deoxycholate-treated purple membrane at 2.6 Å
    • Grigorieff N., Beckmann E., and Zemlin F. Lipid location in deoxycholate-treated purple membrane at 2.6 Å. J. Mol. Biol. 254 (1995) 404-415
    • (1995) J. Mol. Biol. , vol.254 , pp. 404-415
    • Grigorieff, N.1    Beckmann, E.2    Zemlin, F.3
  • 10
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., and Unwin P.N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257 (1975) 28-32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 11
    • 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 J.M., Downing K.H., Lepault J., and Zemlin F. Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 19 (1986) 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
  • 12
    • 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., and Downing K.H. Model for the structure of Bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 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
  • 14
    • 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 global reference structure
    • Kunji E.R., von Gronau S., Oesterhelt D., and Henderson R. 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 (2000) 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
  • 15
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J.A., and Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142 (2003) 334-347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 16
    • 0035782667 scopus 로고    scopus 로고
    • Trimers, dimers of trimers, and trimers of trimers are common building blocks of annexin a5 two-dimensional crystals
    • Oling F., Bergsma-Schutter W., and Brisson A. Trimers, dimers of trimers, and trimers of trimers are common building blocks of annexin a5 two-dimensional crystals. J. Struct. Biol. 133 (2001) 55-63
    • (2001) J. Struct. Biol. , vol.133 , pp. 55-63
    • Oling, F.1    Bergsma-Schutter, W.2    Brisson, A.3
  • 17
    • 0141457531 scopus 로고    scopus 로고
    • Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris
    • Parcej D.N., and Eckhardt-Strelau L. Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris. J. Mol. Biol. 333 (2003) 103-116
    • (2003) J. Mol. Biol. , vol.333 , pp. 103-116
    • Parcej, D.N.1    Eckhardt-Strelau, L.2
  • 20
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., and Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333 (2003) 721-745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 22
    • 27544478958 scopus 로고    scopus 로고
    • Fast maximum-likelihood refinement of electron microscopy images
    • Scheres S.H., Valle M., and Carazo J.M. Fast maximum-likelihood refinement of electron microscopy images. Bioinformatics (Oxford, England) 21 Suppl. 2 (2005) ii243-ii244
    • (2005) Bioinformatics (Oxford, England) , vol.21 , Issue.SUPPL. 2
    • Scheres, S.H.1    Valle, M.2    Carazo, J.M.3
  • 23
    • 0002170585 scopus 로고
    • The theoretical resolution limit of the electron microscope
    • Scherzer O. The theoretical resolution limit of the electron microscope. Appl. Phys. 20 (1948) 20-29
    • (1948) Appl. Phys. , vol.20 , pp. 20-29
    • Scherzer, O.1
  • 24
    • 0027248774 scopus 로고
    • Three-dimensional model of yeast RNA polymerase I determined by electron microscopy of two-dimensional crystals
    • Schultz P., Celia H., Riva M., Sentenac A., and Oudet P. Three-dimensional model of yeast RNA polymerase I determined by electron microscopy of two-dimensional crystals. EMBO J. 12 (1993) 2601-2607
    • (1993) EMBO J. , vol.12 , pp. 2601-2607
    • Schultz, P.1    Celia, H.2    Riva, M.3    Sentenac, A.4    Oudet, P.5
  • 25
    • 0032170383 scopus 로고    scopus 로고
    • Multivariate analysis of single unit cells in electron crystallography
    • Sherman M.B., Soejima T., Chiu W., and van Heel M. Multivariate analysis of single unit cells in electron crystallography. Ultramicroscopy 74 (1998) 179-199
    • (1998) Ultramicroscopy , vol.74 , pp. 179-199
    • Sherman, M.B.1    Soejima, T.2    Chiu, W.3    van Heel, M.4
  • 26
    • 0031704540 scopus 로고    scopus 로고
    • A maximum-likelihood approach to single-particle image refinement
    • Sigworth F.J. A maximum-likelihood approach to single-particle image refinement. J. Struct. Biol. 122 (1998) 328-339
    • (1998) J. Struct. Biol. , vol.122 , pp. 328-339
    • Sigworth, F.J.1
  • 27
    • 0346186102 scopus 로고    scopus 로고
    • Classical detection theory and the cryo-EM particle selection problem
    • Sigworth F.J. Classical detection theory and the cryo-EM particle selection problem. J. Struct. Biol. 145 (2004) 111-122
    • (2004) J. Struct. Biol. , vol.145 , pp. 111-122
    • Sigworth, F.J.1
  • 28
    • 0026663109 scopus 로고
    • Quantitation of molecular densities by cryo-electron microscopy. determination of the radial density distribution of tobacco mosaic virus
    • Smith M.F., and Langmore J.P. Quantitation of molecular densities by cryo-electron microscopy. determination of the radial density distribution of tobacco mosaic virus. J. Mol. Biol. 226 (1992) 763-774
    • (1992) J. Mol. Biol. , vol.226 , pp. 763-774
    • Smith, M.F.1    Langmore, J.P.2
  • 29
    • 0032475911 scopus 로고    scopus 로고
    • Are the light-harvesting I complexes from Rhodospirillum rubrum arranged around the reaction centre in a square geometry?
    • Stahlberg H., Dubochet J., Vogel H., and Ghosh R. Are the light-harvesting I complexes from Rhodospirillum rubrum arranged around the reaction centre in a square geometry?. J. Mol. Biol. 282 (1998) 819-831
    • (1998) J. Mol. Biol. , vol.282 , pp. 819-831
    • Stahlberg, H.1    Dubochet, J.2    Vogel, H.3    Ghosh, R.4
  • 30
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • Stewart A., and Grigorieff N. Noise bias in the refinement of structures derived from single particles. Ultramicroscopy 102 (2004) 67-84
    • (2004) Ultramicroscopy , vol.102 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 31
    • 0033839968 scopus 로고    scopus 로고
    • The 11 A resolution projection map of Na+/K+-ATPase calculated by application of single particle analysis to two-dimensional crystal images
    • Tahara Y., Oshima A., Hirai T., Mitsuoka K., Fujiyoshi Y., and Hayashi Y. The 11 A resolution projection map of Na+/K+-ATPase calculated by application of single particle analysis to two-dimensional crystal images. J. Electron Microsc. (Tokyo) 49 (2000) 583-587
    • (2000) J. Electron Microsc. (Tokyo) , vol.49 , pp. 583-587
    • Tahara, Y.1    Oshima, A.2    Hirai, T.3    Mitsuoka, K.4    Fujiyoshi, Y.5    Hayashi, Y.6
  • 33
    • 0023820449 scopus 로고
    • Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images
    • Toyoshima C., and Unwin N. Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images. Ultramicroscopy 25 (1988) 279-291
    • (1988) Ultramicroscopy , vol.25 , pp. 279-291
    • Toyoshima, C.1    Unwin, N.2
  • 34
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • Toyoshima C., Sasabe H., and Stokes D.L. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 362 (1993) 467-471
    • (1993) Nature , vol.362 , pp. 467-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 35
    • 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 85 (2000) 123-129
    • (2000) Ultramicroscopy , vol.85 , pp. 123-129
    • Vonck, J.1
  • 36
    • 36048973316 scopus 로고    scopus 로고
    • Zhu, J., Frank, J., 1994. Accurate retrieval of transfer function from defocus series. In: Proceedings of the 13th International Congress on Electron Microscopy, Paris, France.
  • 37
    • 0030960710 scopus 로고    scopus 로고
    • Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: procedure and application to the 70S Escherichia coli ribosome
    • Zhu J., Penczek P.A., Schroder R., and Frank J. Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: procedure and application to the 70S Escherichia coli ribosome. J. Struct. Biol. 118 (1997) 197-219
    • (1997) J. Struct. Biol. , vol.118 , pp. 197-219
    • Zhu, J.1    Penczek, P.A.2    Schroder, R.3    Frank, J.4
  • 38
    • 1842418729 scopus 로고    scopus 로고
    • Projection structure and oligomeric state of the osmoregulated sodium/glycine betaine symporter BetP of Corynebacterium glutamicum
    • Ziegler C., Morbach S., Schiller D., Kramer R., Tziatzios C., Schubert D., and Kühlbrandt W. Projection structure and oligomeric state of the osmoregulated sodium/glycine betaine symporter BetP of Corynebacterium glutamicum. J. Mol. Biol. 337 (2004) 1137-1147
    • (2004) J. Mol. Biol. , vol.337 , pp. 1137-1147
    • Ziegler, C.1    Morbach, S.2    Schiller, D.3    Kramer, R.4    Tziatzios, C.5    Schubert, D.6    Kühlbrandt, W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.