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Volumn 26, Issue 1, 2017, Pages 8-15

Atomic resolution structure determination by the cryo-EM method MicroED

Author keywords

cryo EM; crystallography; MicroED; nano crystals

Indexed keywords

CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; PRIORITY JOURNAL; REVIEW; X RAY; X RAY DIFFRACTION; X RAY FREE ELECTRON LASER; PROCEDURES; TRANSMISSION ELECTRON MICROSCOPY; ULTRASTRUCTURE;

EID: 84982242227     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2989     Document Type: Review
Times cited : (21)

References (55)
  • 1
    • 35549001684 scopus 로고    scopus 로고
    • Electronic detectors for electron microscopy
    • Faruqi AR, Henderson R (2007) Electronic detectors for electron microscopy. Curr Opin Struct Biol 17:549–555.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 549-555
    • Faruqi, A.R.1    Henderson, R.2
  • 2
    • 84888087327 scopus 로고    scopus 로고
    • Three-dimensional electron crystallography of protein microcrystals
    • Shi D, Nannenga BL, Iadanza MG, Gonen T (2013) Three-dimensional electron crystallography of protein microcrystals. Elife 2:e01345.
    • (2013) Elife , vol.2
    • Shi, D.1    Nannenga, B.L.2    Iadanza, M.G.3    Gonen, T.4
  • 3
    • 84908434486 scopus 로고    scopus 로고
    • Solving protein nanocrystals by cryo-EM diffraction: multiple scattering artifacts
    • Subramanian G, Basu S, Liu H, Zuo JM, Spence JC (2015) Solving protein nanocrystals by cryo-EM diffraction: multiple scattering artifacts. Ultramicroscopy 148:87–93.
    • (2015) Ultramicroscopy , vol.148 , pp. 87-93
    • Subramanian, G.1    Basu, S.2    Liu, H.3    Zuo, J.M.4    Spence, J.C.5
  • 4
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 A 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 JL, Subramaniam S (2015) 2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science 348:1147–1151.
    • (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
  • 7
    • 84894276173 scopus 로고    scopus 로고
    • High-resolution cryo-electron microscopy on macromolecular complexes and cell organelles
    • Hoenger A (2014) High-resolution cryo-electron microscopy on macromolecular complexes and cell organelles. Protoplasma 251:417–427.
    • (2014) Protoplasma , vol.251 , pp. 417-427
    • Hoenger, A.1
  • 8
    • 84888074636 scopus 로고    scopus 로고
    • Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging
    • Schur FK, Hagen WJ, de Marco A, Briggs JA (2013) Determination of protein structure at 8.5A resolution using cryo-electron tomography and sub-tomogram averaging. J Struct Biol 184:394–400.
    • (2013) J Struct Biol , vol.184 , pp. 394-400
    • Schur, F.K.1    Hagen, W.J.2    de Marco, A.3    Briggs, J.A.4
  • 10
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen T, Sliz P, Kistler J, Cheng Y, Walz T (2004) Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429:193–197.
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 14
    • 84907019355 scopus 로고    scopus 로고
    • High-resolution structure determination by continuous-rotation data collection in MicroED
    • Nannenga BL, Shi D, Leslie AG, Gonen T (2014) High-resolution structure determination by continuous-rotation data collection in MicroED. Nat Methods 11:927–930.
    • (2014) Nat Methods , vol.11 , pp. 927-930
    • Nannenga, B.L.1    Shi, D.2    Leslie, A.G.3    Gonen, T.4
  • 15
    • 84901849376 scopus 로고    scopus 로고
    • A suite of software for processing MicroED data of extremely small protein crystals
    • Iadanza MG, Gonen T (2014) A suite of software for processing MicroED data of extremely small protein crystals. J Appl Crystallogr 47:1140–1145.
    • (2014) J Appl Crystallogr , vol.47 , pp. 1140-1145
    • Iadanza, M.G.1    Gonen, T.2
  • 21
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson R (1995) The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q Rev Biophys 28:171–193.
    • (1995) Q Rev Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 22
    • 77950799462 scopus 로고    scopus 로고
    • The minimum crystal size needed for a complete diffraction data set
    • Holton JM, Frankel KA (2010) The minimum crystal size needed for a complete diffraction data set. Acta Crystallogr D66:393–408.
    • (2010) Acta Crystallogr , vol.D66 , pp. 393-408
    • Holton, J.M.1    Frankel, K.A.2
  • 24
    • 0034680144 scopus 로고    scopus 로고
    • Potential for biomolecular imaging with femtosecond X-ray pulses
    • Neutze R, Wouts R, van der Spoel D, Weckert E, Hajdu J (2000) Potential for biomolecular imaging with femtosecond X-ray pulses. Nature 406:752–757.
    • (2000) Nature , vol.406 , pp. 752-757
    • Neutze, R.1    Wouts, R.2    van der Spoel, D.3    Weckert, E.4    Hajdu, J.5
  • 49
    • 0028659872 scopus 로고
    • Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets
    • Berriman J, Unwin N (1994) Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets. Ultramicroscopy 56:241–252.
    • (1994) Ultramicroscopy , vol.56 , pp. 241-252
    • Berriman, J.1    Unwin, N.2
  • 50
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • Subramaniam S, Gerstein M, Oesterhelt D, Henderson R (1993) Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. Embo J 12:1–8.
    • (1993) Embo J , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 51
    • 84925281992 scopus 로고    scopus 로고
    • Electron crystallography of ultrathin 3D protein crystals: atomic model with charges
    • Yonekura K, Kato K, Ogasawara M, Tomita M, Toyoshima C (2015) Electron crystallography of ultrathin 3D protein crystals: atomic model with charges. Proc Natl Acad Sci USA 112:3368–3373.
    • (2015) Proc Natl Acad Sci USA , vol.112 , pp. 3368-3373
    • Yonekura, K.1    Kato, K.2    Ogasawara, M.3    Tomita, M.4    Toyoshima, C.5
  • 52
    • 84973353644 scopus 로고    scopus 로고
    • Modeling truncated pixel values of faint reflections in MicroED imagesThis article will form part of a virtual special issue of the journal on free-electron laser software
    • [PAGE #S]
    • Hattne J, Shi D, de la Cruz MJ, Reyes FE, Gonen T (2016) Modeling truncated pixel values of faint reflections in MicroED imagesThis article will form part of a virtual special issue of the journal on free-electron laser software. J Appl Crystallogr 49: [PAGE #S].
    • (2016) J Appl Crystallogr , vol.49
    • Hattne, J.1    Shi, D.2    de la Cruz, M.J.3    Reyes, F.E.4    Gonen, T.5
  • 53
    • 0002660809 scopus 로고
    • Detection of sub-units within crystallographic asymmetric unit
    • Rossmann MG, Blow DM (1962) Detection of sub-units within crystallographic asymmetric unit. Acta Crystallogr 15:24.
    • (1962) Acta Crystallogr , vol.15 , pp. 24
    • Rossmann, M.G.1    Blow, D.M.2
  • 54
    • 0000070408 scopus 로고
    • A Fourier series method for the determination of the components of interatomic distances in crystals
    • Patterson AL (1934) A Fourier series method for the determination of the components of interatomic distances in crystals. Phys Rev 46:0372–0376.
    • (1934) Phys Rev , vol.46 , pp. 0372-0376
    • Patterson, A.L.1
  • 55
    • 84884239080 scopus 로고    scopus 로고
    • Cryo-electron tomography: the challenge of doing structural biology in situ
    • Lucic V, Rigort A, Baumeister W (2013) Cryo-electron tomography: the challenge of doing structural biology in situ. J Cell Biol 202:407–419.
    • (2013) J Cell Biol , vol.202 , pp. 407-419
    • Lucic, V.1    Rigort, A.2    Baumeister, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.