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Volumn 195, Issue 2, 2016, Pages 207-215

An algorithm for estimation and correction of anisotropic magnification distortion of cryo-EM images without need of pre-calibration

Author keywords

Anisotropic magnification distortion; Elliptic distortion; Generalized 2 D alignment; jspr; Single particle 3 D reconstruction

Indexed keywords

ALGORITHM; ANISOTROPY; ARTICLE; CALIBRATION; CRYOELECTRON MICROSCOPY; HUMAN; IMAGE ANALYSIS; IMAGE RECONSTRUCTION; MAGNIFICATION RADIOGRAPHY; PARTICLE SIZE; PRIORITY JOURNAL; TRANSMISSION ELECTRON MICROSCOPY; VALIDATION PROCESS; VIRUS MORPHOLOGY; PROCEDURES; THREE DIMENSIONAL IMAGING;

EID: 84992045306     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2016.06.003     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human gamma-secretase
    • e11182
    • Bai, X.C., Rajendra, E., Yang, G., Shi, Y., Scheres, S.H., Sampling the conformational space of the catalytic subunit of human gamma-secretase. Elife, 4, 2015, e11182.
    • (2015) Elife , vol.4
    • Bai, X.C.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.5
  • 3
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 Å resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor
    • Bartesaghi, A., Merk, A., Banerjee, S., Matthies, D., Wu, X., Milne, J.L., Subramaniam, S., 2.2 Å resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science 348 (2015), 1147–1151.
    • (2015) Science , vol.348 , pp. 1147-1151
    • Bartesaghi, A.1    Merk, A.2    Banerjee, S.3    Matthies, D.4    Wu, X.5    Milne, J.L.6    Subramaniam, S.7
  • 5
    • 84924617498 scopus 로고    scopus 로고
    • 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy
    • e06380
    • Campbell, M.G., Veesler, D., Cheng, A., Potter, C.S., Carragher, B., 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy. Elife, 4, 2015, e06380.
    • (2015) Elife , vol.4
    • Campbell, M.G.1    Veesler, D.2    Cheng, A.3    Potter, C.S.4    Carragher, B.5
  • 6
    • 28844509495 scopus 로고    scopus 로고
    • A practical method to detect and correct for lens distortion in the TEM
    • Capitani, G.C., Oleynikov, P., Hovmoller, S., Mellini, M., A practical method to detect and correct for lens distortion in the TEM. Ultramicroscopy 106 (2006), 66–74.
    • (2006) Ultramicroscopy , vol.106 , pp. 66-74
    • Capitani, G.C.1    Oleynikov, P.2    Hovmoller, S.3    Mellini, M.4
  • 7
    • 84923361694 scopus 로고    scopus 로고
    • Atomic structure of T6SS reveals interlaced array essential to function
    • Clemens, D.L., Ge, P., Lee, B.Y., Horwitz, M.A., Zhou, Z.H., Atomic structure of T6SS reveals interlaced array essential to function. Cell 160 (2015), 940–951.
    • (2015) Cell , vol.160 , pp. 940-951
    • Clemens, D.L.1    Ge, P.2    Lee, B.Y.3    Horwitz, M.A.4    Zhou, Z.H.5
  • 8
    • 84946481951 scopus 로고    scopus 로고
    • Automatic estimation and correction of anisotropic magnification distortion in electron microscopes
    • Grant, T., Grigorieff, N., Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J. Struct. Biol. 192 (2015), 204–208.
    • (2015) J. Struct. Biol. , vol.192 , pp. 204-208
    • Grant, T.1    Grigorieff, N.2
  • 9
    • 84930634509 scopus 로고    scopus 로고
    • Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6
    • e06980
    • Grant, T., Grigorieff, N., Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6. Elife, 4, 2015, e06980.
    • (2015) Elife , vol.4
    • Grant, T.1    Grigorieff, N.2
  • 10
    • 84934443131 scopus 로고    scopus 로고
    • Single particle cryo-electron microscopy and 3-D reconstruction of viruses
    • Guo, F., Jiang, W., Single particle cryo-electron microscopy and 3-D reconstruction of viruses. Methods Mol. Biol. 1117 (2014), 401–443.
    • (2014) Methods Mol. Biol. , vol.1117 , pp. 401-443
    • Guo, F.1    Jiang, W.2
  • 13
    • 49549102022 scopus 로고    scopus 로고
    • A DigitalMicrograph™ script to characterize elliptical distortion of electron diffraction patterns in TEM
    • Hou, V., A DigitalMicrograph™ script to characterize elliptical distortion of electron diffraction patterns in TEM. Microsc. Microanal. 14 (2008), 1124–1125.
    • (2008) Microsc. Microanal. , vol.14 , pp. 1124-1125
    • Hou, V.1
  • 14
    • 84930637225 scopus 로고    scopus 로고
    • Atomic structure of anthrax protective antigen pore elucidates toxin translocation
    • Jiang, J., Pentelute, B.L., Collier, R.J., Zhou, Z.H., Atomic structure of anthrax protective antigen pore elucidates toxin translocation. Nature 521 (2015), 545–549.
    • (2015) Nature , vol.521 , pp. 545-549
    • Jiang, J.1    Pentelute, B.L.2    Collier, R.J.3    Zhou, Z.H.4
  • 15
    • 84867904359 scopus 로고    scopus 로고
    • A graph theory method for determination of cryo-EM image focuses
    • Jiang, W., Guo, F., Liu, Z., A graph theory method for determination of cryo-EM image focuses. J. Struct. Biol. 180 (2012), 343–351.
    • (2012) J. Struct. Biol. , vol.180 , pp. 343-351
    • Jiang, W.1    Guo, F.2    Liu, Z.3
  • 16
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X.M., Mooney, P., Zheng, S., Booth, C.R., Braunfeld, M.B., Gubbens, S., Agard, D.A., Cheng, Y.F., Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10 (2013), 584–590.
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.M.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.F.8
  • 17
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D., Cheng, Y., Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504 (2013), 107–112.
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 18
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • Liu, H., Jin, L., Koh, S.B., Atanasov, I., Schein, S., Wu, L., Zhou, Z.H., Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 329 (2010), 1038–1043.
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1    Jin, L.2    Koh, S.B.3    Atanasov, I.4    Schein, S.5    Wu, L.6    Zhou, Z.H.7
  • 19
    • 84954290403 scopus 로고    scopus 로고
    • 2.9 Å resolution Cryo-EM 3D reconstruction of close-packed virus particles
    • Liu, Z., Guo, F., Wang, F., Li, T.C., Jiang, W., 2.9 Å resolution Cryo-EM 3D reconstruction of close-packed virus particles. Structure 24 (2016), 319–328.
    • (2016) Structure , vol.24 , pp. 319-328
    • Liu, Z.1    Guo, F.2    Wang, F.3    Li, T.C.4    Jiang, W.5
  • 20
    • 68549117165 scopus 로고    scopus 로고
    • Accurate and precise lattice parameters by selected-area electron diffraction in the transmission electron microscope
    • Mugnaioli, E., Capitani, G., Nieto, F., Mellini, M., Accurate and precise lattice parameters by selected-area electron diffraction in the transmission electron microscope. Am. Mineral. 94 (2009), 793–800.
    • (2009) Am. Mineral. , vol.94 , pp. 793-800
    • Mugnaioli, E.1    Capitani, G.2    Nieto, F.3    Mellini, M.4
  • 21
    • 0035864288 scopus 로고    scopus 로고
    • The structure of isometric capsids of bacteriophage T4
    • Olson, N.H., Gingery, M., Eiserling, F.A., Baker, T.S., The structure of isometric capsids of bacteriophage T4. Virology 279 (2001), 385–391.
    • (2001) Virology , vol.279 , pp. 385-391
    • Olson, N.H.1    Gingery, M.2    Eiserling, F.A.3    Baker, T.S.4
  • 22
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P.B., 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
  • 23
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S.H., RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180 (2012), 519–530.
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 27
    • 84875362103 scopus 로고    scopus 로고
    • Cryo-EM structure of a novel calicivirus, Tulane virus
    • e59817
    • Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., Jiang, W., Cryo-EM structure of a novel calicivirus, Tulane virus. PLoS One, 8, 2013, e59817.
    • (2013) PLoS One , vol.8
    • Yu, G.1    Zhang, D.2    Guo, F.3    Tan, M.4    Jiang, X.5    Jiang, W.6
  • 28
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu, X., Jin, L., Zhou, Z.H., 3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 453 (2008), 415–419.
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 29
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang, X., Jin, L., Fang, Q., Hui, W.H., Zhou, Z.H., 3.3 Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141 (2010), 472–482.
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 31
    • 84946486192 scopus 로고    scopus 로고
    • Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images
    • Zhao, J., Brubaker, M.A., Benlekbir, S., Rubinstein, J.L., Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images. J. Struct. Biol. 192 (2015), 209–215.
    • (2015) J. Struct. Biol. , vol.192 , pp. 209-215
    • Zhao, J.1    Brubaker, M.A.2    Benlekbir, S.3    Rubinstein, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.