메뉴 건너뛰기




Volumn 192, Issue 2, 2015, Pages 216-221

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

Author keywords

Astigmatism; CTF; Defocus; Phase plate

Indexed keywords

ACCURACY; ALGORITHM; ARTICLE; COMPUTER PROGRAM; CONTRAST TRANSFER FUNCTION; IMAGE ANALYSIS; IMAGE PROCESSING; MATHEMATICAL ANALYSIS; MICROSCOPE; MICROSCOPE DEFOCUS; OPTICAL RESOLUTION; OPTICS; OSCILLATION; PHASE PLATE; PRIORITY JOURNAL; PROCESSING DOSE FRACTIONATION; QUALITY CONTROL; QUALITY OF FIT; TRANSMISSION ELECTRON MICROSCOPY; VELOCITY; IMAGE ENHANCEMENT; PROCEDURES; SOFTWARE; THREE DIMENSIONAL IMAGING;

EID: 84946488108     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2015.08.008     Document Type: Article
Times cited : (3162)

References (14)
  • 1
    • 84905974179 scopus 로고    scopus 로고
    • Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy
    • Bartesaghi A., Matthies D., Banerjee S., Merk A., Subramaniam S. Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy. Proc. Natl. Acad. Sci. 2014, 111:11709-11714. 10.1073/pnas.1402809111.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , pp. 11709-11714
    • Bartesaghi, A.1    Matthies, D.2    Banerjee, S.3    Merk, A.4    Subramaniam, S.5
  • 2
    • 84928379119 scopus 로고    scopus 로고
    • A primer to single-particle cryo-electron microscopy
    • Cheng Y., Grigorieff N., Penczek P., Walz T. A primer to single-particle cryo-electron microscopy. Cell 2015, 161:438-449. 10.1016/j.cell.2015.03.050.
    • (2015) Cell , vol.161 , pp. 438-449
    • Cheng, Y.1    Grigorieff, N.2    Penczek, P.3    Walz, T.4
  • 4
    • 33845326788 scopus 로고    scopus 로고
    • Determination of astigmatism in TEM images
    • Fernando K.V., Fuller S.D. Determination of astigmatism in TEM images. J. Struct. Biol. 2007, 157:189-200.
    • (2007) J. Struct. Biol. , vol.157 , pp. 189-200
    • Fernando, K.V.1    Fuller, S.D.2
  • 5
    • 0344120730 scopus 로고    scopus 로고
    • Automated determination of parameters describing power spectra of micrograph images in electron microscopy
    • 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. 2003, 144:79-94. 10.1016/j.jsb.2003.10.011.
    • (2003) J. Struct. Biol. , vol.144 , pp. 79-94
    • Huang, Z.1    Baldwin, P.R.2    Mullapudi, S.3    Penczek, P.A.4
  • 8
    • 84934905971 scopus 로고    scopus 로고
    • Thon rings from amorphous ice and implications of beam-induced Brownian motion in single particle electron cryo-microscopy
    • McMullan G., Vinothkumar K., Henderson R. Thon rings from amorphous ice and implications of beam-induced Brownian motion in single particle electron cryo-microscopy. Ultramicroscopy 2015, 10.1016/j.ultramic.2015.05.017.
    • (2015) Ultramicroscopy
    • McMullan, G.1    Vinothkumar, K.2    Henderson, R.3
  • 9
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J.A., Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 2003, 142:334-347. 10.1016/S1047-8477(03)00069-8.
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 10
    • 84894283594 scopus 로고    scopus 로고
    • CTER-rapid estimation of CTF parameters with error assessment
    • Penczek P.A., Fang J., Li X., Cheng Y., Loerke J., Spahn C.M.T. CTER-rapid estimation of CTF parameters with error assessment. Ultramicroscopy 2014, 140:9-19. 10.1016/j.ultramic.2014.01.009.
    • (2014) Ultramicroscopy , vol.140 , pp. 9-19
    • Penczek, P.A.1    Fang, J.2    Li, X.3    Cheng, Y.4    Loerke, J.5    Spahn, C.M.T.6
  • 14
    • 33750973339 scopus 로고    scopus 로고
    • Electron energy filtering significantly improves amplitude contrast of frozen-hydrated protein at 300kV
    • Yonekura K., Braunfeld M.B., Maki-Yonekura S., Agard D.A. Electron energy filtering significantly improves amplitude contrast of frozen-hydrated protein at 300kV. J. Struct. Biol. 2006, 156:524-536.
    • (2006) J. Struct. Biol. , vol.156 , pp. 524-536
    • Yonekura, K.1    Braunfeld, M.B.2    Maki-Yonekura, S.3    Agard, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.