메뉴 건너뛰기




Volumn 16, Issue 11, 2019, Pages 1146-1152

Real-time cryo-electron microscopy data preprocessing with Warp

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ;

EID: 85074279272     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/s41592-019-0580-y     Document Type: Article
Times cited : (703)

References (62)
  • 1
    • 84921760682 scopus 로고    scopus 로고
    • A national facility for biological cryo-electron microscopy
    • COI: 1:CAS:528:DC%2BC2MXhsV2gt7w%3D, PID: 25615867
    • Saibil, H. R., Grünewald, K. & Stuart, D. I. A national facility for biological cryo-electron microscopy. Acta Crystallogr. D. 71, 127–135 (2015).
    • (2015) Acta Crystallogr. D. , vol.71 , pp. 127-135
    • Saibil, H.R.1    Grünewald, K.2    Stuart, D.I.3
  • 2
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: the new Leginon system
    • COI: 1:CAS:528:DC%2BD2MXlsFCltbg%3D, PID: 15890530
    • Suloway, C. et al. Automated molecular microscopy: the new Leginon system. J. Struct. Biol. 151, 41–60 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 41-60
    • Suloway, C.1
  • 3
    • 84862783740 scopus 로고    scopus 로고
    • Beam-induced motion of vitrified specimen on holey carbon film
    • COI: 1:CAS:528:DC%2BC38XktlaktLc%3D, PID: 22366277
    • Brilot, A. F. et al. Beam-induced motion of vitrified specimen on holey carbon film. J. Struct. Biol. 177, 630–637 (2012).
    • (2012) J. Struct. Biol. , vol.177 , pp. 630-637
    • Brilot, A.F.1
  • 4
    • 0344120730 scopus 로고    scopus 로고
    • Automated determination of parameters describing power spectra of micrograph images in electron microscopy
    • PID: 14643211
    • Huang, Z., Baldwin, P. R., Mullapudi, S. & Penczek, P. A. Automated determination of parameters describing power spectra of micrograph images in electron microscopy. J. Struct. Biol. 144, 79–94 (2003).
    • (2003) J. Struct. Biol. , vol.144 , pp. 79-94
    • Huang, Z.1    Baldwin, P.R.2    Mullapudi, S.3    Penczek, P.A.4
  • 5
    • 0020014750 scopus 로고
    • Detection of objects in quantum-noise-limited images
    • van Heel, M. Detection of objects in quantum-noise-limited images. Ultramicroscopy 7, 331–341 (1982).
    • (1982) Ultramicroscopy , vol.7 , pp. 331-341
    • van Heel, M.1
  • 6
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • COI: 1:CAS:528:DC%2BC3sXntVakur0%3D, PID: 23644547
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584–590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 7
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6
    • PID: 26023829
    • Grant, T. & Grigorieff, N. Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6. eLife 4, e06980 (2015).
    • (2015) eLife , vol.4
    • Grant, T.1    Grigorieff, N.2
  • 8
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • PID: 16182563
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36–51 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 9
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • COI: 1:CAS:528:DC%2BC2sXjt1ags7g%3D, PID: 28250466
    • Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331–332 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1
  • 10
    • 84946473054 scopus 로고    scopus 로고
    • Alignment of cryo-EM movies of individual particles by optimization of image translations
    • PID: 26296328
    • Rubinstein, J. L. & Brubaker, M. A. Alignment of cryo-EM movies of individual particles by optimization of image translations. J. Struct. Biol. 192, 188–195 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 188-195
    • Rubinstein, J.L.1    Brubaker, M.A.2
  • 11
    • 85009291685 scopus 로고    scopus 로고
    • Robust image alignment for cryogenic transmission electron microscopy
    • COI: 1:CAS:528:DC%2BC2sXjvFaqtA%3D%3D, PID: 28038834
    • McLeod, R. A., Kowal, J., Ringler, P. & Stahlberg, H. Robust image alignment for cryogenic transmission electron microscopy. J. Struct. Biol. 197, 279–293 (2017).
    • (2017) J. Struct. Biol. , vol.197 , pp. 279-293
    • McLeod, R.A.1    Kowal, J.2    Ringler, P.3    Stahlberg, H.4
  • 12
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: Fast and accurate defocus estimation from electron micrographs
    • PID: 26278980
    • Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216–221 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 13
    • 84959182065 scopus 로고    scopus 로고
    • High resolution single particle refinement in EMAN2.1
    • COI: 1:CAS:528:DC%2BC28XjsVaqsbw%3D
    • Bell, J. M., Chen, M., Baldwin, P. R. & Ludtke, S. J. High resolution single particle refinement in EMAN2.1. Methods (San. Diego, Calif.) 100, 25–34 (2016).
    • (2016) Methods (San. Diego, Calif.) , vol.100 , pp. 25-34
    • Bell, J.M.1    Chen, M.2    Baldwin, P.R.3    Ludtke, S.J.4
  • 14
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: Real-time CTF determination and correction
    • COI: 1:CAS:528:DC%2BC2MXhvVOqsbzF, PID: 26592709
    • Zhang, K. Gctf: Real-time CTF determination and correction. J. Struct. Biol. 193, 1–12 (2016).
    • (2016) J. Struct. Biol. , vol.193 , pp. 1-12
    • Zhang, K.1
  • 15
    • 84922727036 scopus 로고    scopus 로고
    • Semi-automated selection of cryo-EM particles in RELION-1.3
    • COI: 1:CAS:528:DC%2BC2cXitV2ms7bI, PID: 25486611
    • Scheres, S. H. Semi-automated selection of cryo-EM particles in RELION-1.3. J. Struct. Biol. 189, 114–122 (2015).
    • (2015) J. Struct. Biol. , vol.189 , pp. 114-122
    • Scheres, S.H.1
  • 16
    • 0346816491 scopus 로고    scopus 로고
    • FindEM-a fast, efficient program for automatic selection of particles from electron micrographs
    • COI: 1:CAS:528:DC%2BD2cXjtVCmsQ%3D%3D, PID: 15065677
    • Roseman, A. M. FindEM-a fast, efficient program for automatic selection of particles from electron micrographs. J. Struct. Biol. 145, 91–99 (2004).
    • (2004) J. Struct. Biol. , vol.145 , pp. 91-99
    • Roseman, A.M.1
  • 17
    • 33845449481 scopus 로고    scopus 로고
    • SIGNATURE: a single-particle selection system for molecular electron microscopy
    • COI: 1:CAS:528:DC%2BD28XhtlaltrbK, PID: 16870473
    • Chen, J. Z. & Grigorieff, N. SIGNATURE: a single-particle selection system for molecular electron microscopy. J. Struct. Biol. 157, 168–173 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 18
    • 67651054955 scopus 로고    scopus 로고
    • Automatic particle selection from electron micrographs using machine learning techniques
    • COI: 1:STN:280:DC%2BD1MrhtF2ktA%3D%3D, PID: 19555764
    • Sorzano, C. et al. Automatic particle selection from electron micrographs using machine learning techniques. J. Struct. Biol. 167, 252–260 (2009).
    • (2009) J. Struct. Biol. , vol.167 , pp. 252-260
    • Sorzano, C.1
  • 19
    • 84991394143 scopus 로고    scopus 로고
    • DeepPicker: A deep learning approach for fully automated particle picking in cryo-EM
    • PID: 27424268
    • Wang, F. et al. DeepPicker: A deep learning approach for fully automated particle picking in cryo-EM. J. Struct. Biol. 195, 325–336 (2016).
    • (2016) J. Struct. Biol. , vol.195 , pp. 325-336
    • Wang, F.1
  • 20
    • 60649103238 scopus 로고    scopus 로고
    • Appion: an integrated, database-driven pipeline to facilitate EM image processing
    • COI: 1:CAS:528:DC%2BD1MXisFSktLY%3D, PID: 19263523
    • Lander, G. C. et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. J. Struct. Biol. 166, 95–102 (2009).
    • (2009) J. Struct. Biol. , vol.166 , pp. 95-102
    • Lander, G.C.1
  • 21
    • 85018192388 scopus 로고    scopus 로고
    • Focus: The interface between data collection and data processing in cryo-EM
    • COI: 1:CAS:528:DC%2BC2sXmvFSlt7g%3D, PID: 28344036
    • Biyani, N. et al. Focus: The interface between data collection and data processing in cryo-EM. J. Struct. Biol. 198, 124–133 (2017).
    • (2017) J. Struct. Biol. , vol.198 , pp. 124-133
    • Biyani, N.1
  • 22
    • 84964290813 scopus 로고    scopus 로고
    • Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy
    • PID: 27108186
    • de la Rosa-Trevin, J. M. et al. Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy. J. Struct. Biol. 195, 93–99 (2016).
    • (2016) J. Struct. Biol. , vol.195 , pp. 93-99
    • de la Rosa-Trevin, J.M.1
  • 23
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • COI: 1:CAS:528:DC%2BC38Xhs12jsLvO, PID: 23000701
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 24
    • 85011645437 scopus 로고    scopus 로고
    • cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
    • COI: 1:CAS:528:DC%2BC2sXitlGisbs%3D, PID: 28165473
    • Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination. Nat. Methods 14, 290 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 290
    • Punjani, A.1    Rubinstein, J.L.2    Fleet, D.J.3    Brubaker, M.A.4
  • 25
    • 85026485285 scopus 로고    scopus 로고
    • Addressing preferred specimen orientation in single-particle cryo-EM through tilting
    • COI: 1:CAS:528:DC%2BC2sXhtFSmtrjO, PID: 28671674
    • Tan, Y. Z. et al. Addressing preferred specimen orientation in single-particle cryo-EM through tilting. Nat. Methods 14, 793–796 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 793-796
    • Tan, Y.Z.1
  • 26
    • 85006371642 scopus 로고    scopus 로고
    • Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution subtomogram averaging
    • PID: 27313000
    • Hagen, W. J. H., Wan, W. & Briggs, J. A. G. Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution subtomogram averaging. J. Struct. Biol. 197, 191–198 (2017).
    • (2017) J. Struct. Biol. , vol.197 , pp. 191-198
    • Hagen, W.J.H.1    Wan, W.2    Briggs, J.A.G.3
  • 27
    • 84868573207 scopus 로고    scopus 로고
    • Movies of ice-embedded particles enhance resolution in electron cryo-microscopy
    • COI: 1:CAS:528:DC%2BC38XhsVaqtbvM, PID: 23022349
    • Campbell, M. G. et al. Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. Structure 20, 1823–1828 (2012).
    • (2012) Structure , vol.20 , pp. 1823-1828
    • Campbell, M.G.1
  • 28
    • 85051955816 scopus 로고    scopus 로고
    • Routine single particle cryoem sample and grid characterization by tomography
    • PID: 29809143
    • Noble, A. J. et al. Routine single particle cryoem sample and grid characterization by tomography. eLife 7, e34257 (2018).
    • (2018) eLife , vol.7
    • Noble, A.J.1
  • 29
    • 0032203257 scopus 로고    scopus 로고
    • Gradient-based learning applied to document recognition
    • Lecun, Y., Bottou, L., Bengio, Y. & Haffner, P. Gradient-based learning applied to document recognition. Proc. IEEE 86, 2278–2324 (1998).
    • (1998) Proc. IEEE , vol.86 , pp. 2278-2324
    • Lecun, Y.1    Bottou, L.2    Bengio, Y.3    Haffner, P.4
  • 33
    • 84961393393 scopus 로고    scopus 로고
    • EMPIAR: a public archive for raw electron microscopy image data
    • COI: 1:CAS:528:DC%2BC28XksFCrtbc%3D, PID: 27067018
    • Iudin, A., Korir, P. K., Salavert-Torres, J., Kleywegt, G. J. & Patwardhan, A. EMPIAR: a public archive for raw electron microscopy image data. Nat. Methods 13, 387–388 (2016).
    • (2016) Nat. Methods , vol.13 , pp. 387-388
    • Iudin, A.1    Korir, P.K.2    Salavert-Torres, J.3    Kleywegt, G.J.4    Patwardhan, A.5
  • 34
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • COI: 1:CAS:528:DC%2BD3cXhvVKjt7w%3D, PID: 102472
    • Berman, H. M. et al. The Protein Data Bank. Nucleic Acids Res. 28, 235–242 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 35
    • 85071181136 scopus 로고    scopus 로고
    • SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM
    • PID: 31240256
    • Wagner, T. et al. SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM. Commun. Biol. 2, 218 (2019).
    • (2019) Commun. Biol. , vol.2 , pp. 218
    • Wagner, T.1
  • 36
    • 85056950318 scopus 로고    scopus 로고
    • RELION-3: new tools for automated high-resolution cryo-EM structure determination
    • PID: 30412051
    • Zivanov, J. et al. RELION-3: new tools for automated high-resolution cryo-EM structure determination. eLife 7, e42166 (2018).
    • (2018) eLife , vol.7
    • Zivanov, J.1
  • 37
    • 0036848127 scopus 로고    scopus 로고
    • New electron microscopy database and deposition system
    • COI: 1:CAS:528:DC%2BD38Xotlykt7Y%3D, PID: 12417136
    • Tagari, M., Newman, R., Chagoyen, M., Carazo, J. M. & Henrick, K. New electron microscopy database and deposition system. Trends Biochem. Sci. 27, 589 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 589
    • Tagari, M.1    Newman, R.2    Chagoyen, M.3    Carazo, J.M.4    Henrick, K.5
  • 38
    • 84887271303 scopus 로고    scopus 로고
    • Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise
    • COI: 1:CAS:528:DC%2BC3sXhvVSmurzE, PID: 24106306
    • Henderson, R. Avoiding the pitfalls of single particle cryo-electron microscopy: Einstein from noise. Proc. Natl Acad. Sci. USA 110, 18037–18041 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 18037-18041
    • Henderson, R.1
  • 39
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor
    • COI: 1:CAS:528:DC%2BC2MXpt1KlsL4%3D, PID: 25953817
    • Bartesaghi, A. et al. 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science 348, 1147–1151 (2015).
    • (2015) Science , vol.348 , pp. 1147-1151
    • Bartesaghi, A.1
  • 40
    • 84992573769 scopus 로고    scopus 로고
    • Resolving macromolecular structures from electron cryo-tomography data using subtomogram averaging in RELION
    • COI: 1:CAS:528:DC%2BC28XhsF2mtLrL, PID: 27685097
    • Bharat, T. A. & Scheres, S. H. Resolving macromolecular structures from electron cryo-tomography data using subtomogram averaging in RELION. Nat. Protoc. 11, 2054–2065 (2016).
    • (2016) Nat. Protoc. , vol.11 , pp. 2054-2065
    • Bharat, T.A.1    Scheres, S.H.2
  • 41
    • 85026294137 scopus 로고    scopus 로고
    • Efficient 3D-CTF correction for cryo-electron tomography using NovaCTF improves subtomogram averaging resolution to 3.4A
    • COI: 1:CAS:528:DC%2BC2sXht1CrsL%2FM, PID: 28743638
    • Turonova, B., Schur, F. K. M., Wan, W. & Briggs, J. A. G. Efficient 3D-CTF correction for cryo-electron tomography using NovaCTF improves subtomogram averaging resolution to 3.4A. J. Struct. Biol. 199, 187–195 (2017).
    • (2017) J. Struct. Biol. , vol.199 , pp. 187-195
    • Turonova, B.1    Schur, F.K.M.2    Wan, W.3    Briggs, J.A.G.4
  • 42
    • 84966262179 scopus 로고
    • Updating quasi-Newton matrices with limited storage
    • Nocedal, J. Updating quasi-Newton matrices with limited storage. Math. Comput. 35, 773–773 (1980).
    • (1980) Math. Comput. , vol.35 , pp. 773
    • Nocedal, J.1
  • 43
    • 65649120376 scopus 로고    scopus 로고
    • Error analysis in the determination of the electron microscopical contrast transfer function parameters from experimental power Spectra
    • PID: 19321015
    • Sorzano, C. O., Otero, A., Olmos, E. M. & Carazo, J. M. Error analysis in the determination of the electron microscopical contrast transfer function parameters from experimental power Spectra. BMC Struct. Biol. 9, 18 (2009).
    • (2009) BMC Struct. Biol. , vol.9
    • Sorzano, C.O.1    Otero, A.2    Olmos, E.M.3    Carazo, J.M.4
  • 44
    • 84894283594 scopus 로고    scopus 로고
    • CTER—Rapid estimation of CTF parameters with error assessment
    • COI: 1:CAS:528:DC%2BC2cXmtVajsL0%3D, PID: 24562077
    • Penczek, P. A. et al. CTER—Rapid estimation of CTF parameters with error assessment. Ultramicroscopy 140, 9–19 (2014).
    • (2014) Ultramicroscopy , vol.140 , pp. 9-19
    • Penczek, P.A.1
  • 45
    • 85011422346 scopus 로고    scopus 로고
    • Using the Volta phase plate with defocus for cryo-EM single particle analysis
    • PID: 28109158
    • Danev, R., Tegunov, D. & Baumeister, W. Using the Volta phase plate with defocus for cryo-EM single particle analysis. eLife 6, e23006 (2017).
    • (2017) eLife , vol.6
    • Danev, R.1    Tegunov, D.2    Baumeister, W.3
  • 46
    • 79960010288 scopus 로고    scopus 로고
    • A fast algorithm for computing and correcting the CTF for tilted, thick specimens in TEM
    • COI: 1:CAS:528:DC%2BC3MXhtVGlsrfP, PID: 21740865
    • Voortman, L. M., Stallinga, S., Schoenmakers, R. H. M., Vliet, L. Jv & Rieger, B. A fast algorithm for computing and correcting the CTF for tilted, thick specimens in TEM. Ultramicroscopy 111, 1029–1036 (2011).
    • (2011) Ultramicroscopy , vol.111 , pp. 1029-1036
    • Voortman, L.M.1    Stallinga, S.2    Schoenmakers, R.H.M.3    Vliet, L.J.4    Rieger, B.5
  • 47
    • 84978785861 scopus 로고    scopus 로고
    • An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation
    • COI: 1:CAS:528:DC%2BC28Xht1ehtL%2FN, PID: 27417497
    • Schur, F. K. et al. An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. Science 353, 506–508 (2016).
    • (2016) Science , vol.353 , pp. 506-508
    • Schur, F.K.1
  • 49
    • 84947019114 scopus 로고    scopus 로고
    • Advances in Single-Particle Electron Cryomicroscopy Structure Determination applied to Sub-tomogram Averaging
    • COI: 1:CAS:528:DC%2BC2MXhtlSju7jI, PID: 26256537
    • Bharat, T. A., Russo, C. J., Lowe, J., Passmore, L. A. & Scheres, S. H. Advances in Single-Particle Electron Cryomicroscopy Structure Determination applied to Sub-tomogram Averaging. Structure 23, 1743–1753 (2015).
    • (2015) Structure , vol.23 , pp. 1743-1753
    • Bharat, T.A.1    Russo, C.J.2    Lowe, J.3    Passmore, L.A.4    Scheres, S.H.5
  • 50
    • 85054559719 scopus 로고    scopus 로고
    • Subtomogram averaging of COPII assemblies reveals how coat organization dictates membrane shape
    • PID: 30297805
    • Hutchings, J., Stancheva, V., Miller, E. A. & Zanetti, G. Subtomogram averaging of COPII assemblies reveals how coat organization dictates membrane shape. Nat. Commun. 9, 4154 (2018).
    • (2018) Nat. Commun. , vol.9
    • Hutchings, J.1    Stancheva, V.2    Miller, E.A.3    Zanetti, G.4
  • 51
    • 85041413051 scopus 로고    scopus 로고
    • Ewald sphere correction using a single side-band image processing algorithm
    • COI: 1:CAS:528:DC%2BC1cXisVahsb0%3D, PID: 29413409
    • Russo, C. J. & Henderson, R. Ewald sphere correction using a single side-band image processing algorithm. Ultramicroscopy 187, 26–33 (2018).
    • (2018) Ultramicroscopy , vol.187 , pp. 26-33
    • Russo, C.J.1    Henderson, R.2
  • 52
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • COI: 1:CAS:528:DC%2BD28XhtlaltrbN, PID: 16828314
    • Grigorieff, N. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 157, 117–125 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 53
    • 85003534346 scopus 로고    scopus 로고
    • Three-dimensional CTF correction improves the resolution of electron tomograms
    • PID: 27343995
    • Kunz, M. & Frangakis, A. S. Three-dimensional CTF correction improves the resolution of electron tomograms. J. Struct. Biol. 197, 114–122 (2017).
    • (2017) J. Struct. Biol. , vol.197 , pp. 114-122
    • Kunz, M.1    Frangakis, A.S.2
  • 54
    • 84946481951 scopus 로고    scopus 로고
    • Automatic estimation and correction of anisotropic magnification distortion in electron microscopes
    • PID: 26278979
    • Grant, T. & Grigorieff, N. Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J. Struct. Biol. 192, 204–208 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 204-208
    • Grant, T.1    Grigorieff, N.2
  • 55
    • 23044475632 scopus 로고    scopus 로고
    • Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology
    • PID: 16043364
    • Heymann, J. B., Chagoyen, M. & Belnap, D. M. Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology. J. Struct. Biol. 151, 196–207 (2005).
    • (2005) J. Struct. Biol. , vol.151 , pp. 196-207
    • Heymann, J.B.1    Chagoyen, M.2    Belnap, D.M.3
  • 56
    • 84951834022 scopus 로고    scopus 로고
    • U-Net: Convolutional Networks for Biomedical Image Segmentation
    • (eds N., Navab et al.) Vol, , (Springer, 2015)
    • Ronneberger, O., Fischer, P. & Brox, T. U-Net: Convolutional Networks for Biomedical Image Segmentation. In MICCAI 2015 Lecture Notes in Computer Science (eds N., Navab et al.) Vol 9351, 234–241 (Springer, 2015).
    • MICCAI 2015 Lecture Notes in Computer Science , vol.9351 , pp. 234-241
    • Ronneberger, O.1    Fischer, P.2    Brox, T.3
  • 57
    • 84879890758 scopus 로고    scopus 로고
    • Image formation modeling in cryo-electron microscopy
    • COI: 1:CAS:528:DC%2BC3sXhtVKru7fP, PID: 23711417
    • Vulovic, M. et al. Image formation modeling in cryo-electron microscopy. J. Struct. Biol. 183, 19–32 (2013).
    • (2013) J. Struct. Biol. , vol.183 , pp. 19-32
    • Vulovic, M.1
  • 58
    • 85020436942 scopus 로고    scopus 로고
    • Single-protein detection in crowded molecular environments in cryo-EM images
    • PID: 28467302
    • Rickgauer, J. P., Grigorieff, N. & Denk, W. Single-protein detection in crowded molecular environments in cryo-EM images. eLife 6, e25648 (2017).
    • (2017) eLife , vol.6
    • Rickgauer, J.P.1    Grigorieff, N.2    Denk, W.3
  • 59
    • 85018922091 scopus 로고    scopus 로고
    • Image restoration using convolutional auto-encoders with symmetric skip connections
    • Mao, X.-J., Shen, C. & Yang, Y.-B. Image restoration using convolutional auto-encoders with symmetric skip connections. Adv. Neural Inform. Proc. Syst. 29, 2802–2810 (2016).
    • (2016) Adv. Neural Inform. Proc. Syst. , vol.29 , pp. 2802-2810
    • Mao, X.-J.1    Shen, C.2    Yang, Y.-B.3
  • 62
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • COI: 1:STN:280:DyaK28zmtFyqtg%3D%3D, PID: 8742726
    • Kremer, J. R., Mastronarde, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71–76 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.