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Volumn 157, Issue 1, 2007, Pages 3-18

Bsoft: Image processing and molecular modeling for electron microscopy

Author keywords

Distributed processing; Image processing workflow; Single particle analysis; Three dimensional image reconstruction; Tomography

Indexed keywords

AMINO ACID; NUCLEIC ACID;

EID: 33845336533     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.06.006     Document Type: Article
Times cited : (428)

References (40)
  • 1
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T.S., and Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116 (1996) 120-130
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 2
    • 0034406521 scopus 로고    scopus 로고
    • Macromolecular electron microscopy in the era of structural genomics
    • Baumeister W., and Steven A.C. Macromolecular electron microscopy in the era of structural genomics. Trends Biochem. Sci. 25 (2000) 624-631
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 624-631
    • Baumeister, W.1    Steven, A.C.2
  • 3
    • 0027556541 scopus 로고
    • Use of radial density plots to calibrate image magnification for frozen-hydrated specimens
    • Belnap D.M., Grochulski W.D., Olson N.H., and Baker T.S. Use of radial density plots to calibrate image magnification for frozen-hydrated specimens. Ultramicroscopy 48 (1993) 347-358
    • (1993) Ultramicroscopy , vol.48 , pp. 347-358
    • Belnap, D.M.1    Grochulski, W.D.2    Olson, N.H.3    Baker, T.S.4
  • 4
    • 0031257718 scopus 로고    scopus 로고
    • A method for establishing the handedness of biological macromolecules
    • Belnap D.M., Olson N.H., and Baker T.S. A method for establishing the handedness of biological macromolecules. J. Struct. Biol. 120 (1997) 44-51
    • (1997) J. Struct. Biol. , vol.120 , pp. 44-51
    • Belnap, D.M.1    Olson, N.H.2    Baker, T.S.3
  • 6
    • 17044373783 scopus 로고    scopus 로고
    • The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes
    • Bubeck D., Filman D.J., Cheng N., Steven A.C., Hogle J.M., and Belnap D.M. The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes. J. Virol. 79 (2005) 7745-7755
    • (2005) J. Virol. , vol.79 , pp. 7745-7755
    • Bubeck, D.1    Filman, D.J.2    Cheng, N.3    Steven, A.C.4    Hogle, J.M.5    Belnap, D.M.6
  • 9
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A., Amos L.A., Finch J.T., De Rosier D.J., and Klug A. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 226 (1970) 421-425
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    De Rosier, D.J.4    Klug, A.5
  • 10
    • 0344983333 scopus 로고    scopus 로고
    • Web portal to an image database for high-resolution three-dimensional reconstruction
    • Dai W., Liang Y., and Zhou Z.H. Web portal to an image database for high-resolution three-dimensional reconstruction. J. Struct. Biol. 144 (2003) 238-245
    • (2003) J. Struct. Biol. , vol.144 , pp. 238-245
    • Dai, W.1    Liang, Y.2    Zhou, Z.H.3
  • 11
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 12
    • 0343052627 scopus 로고    scopus 로고
    • A spectral estimation approach to contrast transfer function detection in electron microscopy
    • Fernandez J.-J., Sanjurjo J., and Carazo J.-M. A spectral estimation approach to contrast transfer function detection in electron microscopy. Ultramicroscopy 68 (1997) 267
    • (1997) Ultramicroscopy , vol.68 , pp. 267
    • Fernandez, J.-J.1    Sanjurjo, J.2    Carazo, J.-M.3
  • 13
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis A.S., and Hegerl R. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 135 (2001) 239-250
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 14
    • 0019802812 scopus 로고
    • Computer averaging of electron micrographs of 40S ribosomal subunits
    • Frank J., Verschoor A., and Boublik M. Computer averaging of electron micrographs of 40S ribosomal subunits. Science 214 (1981) 1353-1355
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 15
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles-the uncommon line
    • Fuller S.D., Butcher S.J., Cheng R.H., and Baker T.S. Three-dimensional reconstruction of icosahedral particles-the uncommon line. J. Struct. Biol. 116 (1996) 48-55
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 17
    • 0001078409 scopus 로고
    • The STAR file: a new format for electronic data transfer and archiving
    • Hall S.R. The STAR file: a new format for electronic data transfer and archiving. J. Chem. Inf. Comput. Sci. 31 (1991) 326-333
    • (1991) J. Chem. Inf. Comput. Sci. , vol.31 , pp. 326-333
    • Hall, S.R.1
  • 18
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz G., and van Heel M. Exact filters for general geometry three dimensional reconstruction. Optik 73 (1986) 146-156
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 19
    • 0035783171 scopus 로고    scopus 로고
    • Bsoft: image and molecular processing in electron microscopy
    • Heymann J.B. Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133 (2001) 156-169
    • (2001) J. Struct. Biol. , vol.133 , pp. 156-169
    • Heymann, J.B.1
  • 20
    • 0034723156 scopus 로고    scopus 로고
    • Structural clues in the sequences of the aquaporins
    • Heymann J.B., and Engel A. Structural clues in the sequences of the aquaporins. J. Mol. Biol. 295 (2000) 1039-1053
    • (2000) J. Mol. Biol. , vol.295 , pp. 1039-1053
    • Heymann, J.B.1    Engel, A.2
  • 23
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
    • Heymann J.B., Cheng N., Newcomb W.W., Trus B.L., Brown J.C., and Steven A.C. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat. Struct. Biol. 10 (2003) 334-341
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 24
    • 4344664583 scopus 로고    scopus 로고
    • Molecular dynamics of protein complexes from four-dimensional cryo-electron microscopy
    • Heymann J.B., Conway J.F., and Steven A.C. Molecular dynamics of protein complexes from four-dimensional cryo-electron microscopy. J. Struct. Biol. 147 (2004) 291-301
    • (2004) J. Struct. Biol. , vol.147 , pp. 291-301
    • Heymann, J.B.1    Conway, J.F.2    Steven, A.C.3
  • 25
    • 23044475632 scopus 로고    scopus 로고
    • Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology
    • (Corrigendum, J. Struct. Biol. 153, 312)
    • Heymann J.B., Chagoyen M., and Belnap D.M. Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology. J. Struct. Biol. 151 (2005) 196-207 (Corrigendum, J. Struct. Biol. 153, 312)
    • (2005) J. Struct. Biol. , vol.151 , pp. 196-207
    • Heymann, J.B.1    Chagoyen, M.2    Belnap, D.M.3
  • 27
    • 4344559453 scopus 로고    scopus 로고
    • The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes
    • Huiskonen J.T., Kivela H.M., Bamford D.H., and Butcher S.J. The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. Nat. Struct. Mol. Biol. 11 (2004) 850-856
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 850-856
    • Huiskonen, J.T.1    Kivela, H.M.2    Bamford, D.H.3    Butcher, S.J.4
  • 29
    • 32544437801 scopus 로고    scopus 로고
    • A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography
    • Iancu C.V., Wright E.R., Heymann J.B., and Jensen G.J. A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography. J. Struct. Biol. 153 (2006) 231-240
    • (2006) J. Struct. Biol. , vol.153 , pp. 231-240
    • Iancu, C.V.1    Wright, E.R.2    Heymann, J.B.3    Jensen, G.J.4
  • 30
    • 0031853365 scopus 로고    scopus 로고
    • Fast computation of 3D radon transform via a direct Fourier method
    • Lanzavecchia S., and Luigi Bellon P. Fast computation of 3D radon transform via a direct Fourier method. Bioinformatics 14 (1998) 212-216
    • (1998) Bioinformatics , vol.14 , pp. 212-216
    • Lanzavecchia, S.1    Luigi Bellon, P.2
  • 31
    • 0033572575 scopus 로고    scopus 로고
    • Fast and accurate three-dimensional reconstruction from projections with random orientations via radon transforms
    • Lanzavecchia S., Bellon P.L., and Radermacher M. Fast and accurate three-dimensional reconstruction from projections with random orientations via radon transforms. J. Struct. Biol. 128 (1999) 152-164
    • (1999) J. Struct. Biol. , vol.128 , pp. 152-164
    • Lanzavecchia, S.1    Bellon, P.L.2    Radermacher, M.3
  • 32
    • 17044371193 scopus 로고    scopus 로고
    • Peach: a simple Perl-based system for distributed computation and its application to cryo-EM data processing
    • Leong P.A., Heymann J.B., and Jensen G.J. Peach: a simple Perl-based system for distributed computation and its application to cryo-EM data processing. Structure 13 (2005) 505-511
    • (2005) Structure , vol.13 , pp. 505-511
    • Leong, P.A.1    Heymann, J.B.2    Jensen, G.J.3
  • 33
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 34
    • 0942299966 scopus 로고    scopus 로고
    • Object oriented database and electronic notebook for transmission electron microscopy
    • Ludtke S.J., Nason L., Tu H., Peng L., and Chiu W. Object oriented database and electronic notebook for transmission electron microscopy. Microsc. Microanal. 9 (2003) 556-565
    • (2003) Microsc. Microanal. , vol.9 , pp. 556-565
    • Ludtke, S.J.1    Nason, L.2    Tu, H.3    Peng, L.4    Chiu, W.5
  • 35
    • 0035783254 scopus 로고    scopus 로고
    • Adopting a database as a solution to managing electron image data
    • Metoz F., Sherman M.B., and Schmid M.F. Adopting a database as a solution to managing electron image data. J. Struct. Biol. 133 (2001) 170-175
    • (2001) J. Struct. Biol. , vol.133 , pp. 170-175
    • Metoz, F.1    Sherman, M.B.2    Schmid, M.F.3
  • 36
    • 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
  • 37
    • 28844462954 scopus 로고    scopus 로고
    • Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes
    • Murphy G.E., and Jensen G.J. Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes. Structure 13 (2005) 1765-1773
    • (2005) Structure , vol.13 , pp. 1765-1773
    • Murphy, G.E.1    Jensen, G.J.2
  • 38
    • 0035120433 scopus 로고    scopus 로고
    • Capsid structure of Kaposi's sarcoma-associated herpesvirus, a gammaherpesvirus, compared to an alphaherpesvirus, HSV1, and a betaherpesvirus, CMV
    • Trus B.L., Heymann J.B., Nealon K., Cheng N., Newcomb W.W., Brown J.C., Kedes D.H., and Steven A.C. Capsid structure of Kaposi's sarcoma-associated herpesvirus, a gammaherpesvirus, compared to an alphaherpesvirus, HSV1, and a betaherpesvirus, CMV. J. Virol. 75 (2001) 2879-2890
    • (2001) J. Virol. , vol.75 , pp. 2879-2890
    • Trus, B.L.1    Heymann, J.B.2    Nealon, K.3    Cheng, N.4    Newcomb, W.W.5    Brown, J.C.6    Kedes, D.H.7    Steven, A.C.8
  • 39
    • 0035787907 scopus 로고    scopus 로고
    • Do single (ribosome) molecules phase themselves?
    • van Heel M. Do single (ribosome) molecules phase themselves?. Cold Spring Harb. Symp. Quant. Biol. 66 (2001) 77-86
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 77-86
    • van Heel, M.1
  • 40
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.