메뉴 건너뛰기




Volumn 100, Issue , 2016, Pages 3-15

An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology

Author keywords

Electron microscopy

Indexed keywords

QUANTUM DOT;

EID: 84961135724     PISSN: 10462023     EISSN: 10959130     Source Type: Journal    
DOI: 10.1016/j.ymeth.2016.02.017     Document Type: Article
Times cited : (184)

References (117)
  • 1
    • 84876044174 scopus 로고    scopus 로고
    • Single particle electron microscopy
    • Lau W.C.Y., Rubinstein J.L. Single particle electron microscopy. Methods Mol. Biol. 2013, 955:401-426. 10.1007/978-1-62703-176-9_22.
    • (2013) Methods Mol. Biol. , vol.955 , pp. 401-426
    • Lau, W.C.Y.1    Rubinstein, J.L.2
  • 2
    • 84928379119 scopus 로고    scopus 로고
    • A primer to single-particle cryo-electron microscopy
    • Cheng Y., Grigorieff N., Penczek P.A., 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.A.3    Walz, T.4
  • 3
    • 84939260439 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of helical polymers
    • Egelman E.H. Three-dimensional reconstruction of helical polymers. Arch. Biochem. Biophys. 2015, 581:54-58. 10.1016/j.abb.2015.04.004.
    • (2015) Arch. Biochem. Biophys. , vol.581 , pp. 54-58
    • Egelman, E.H.1
  • 4
    • 84878527131 scopus 로고    scopus 로고
    • Structural biology in situ - the potential of subtomogram averaging
    • Briggs J.A.G. Structural biology in situ - the potential of subtomogram averaging. Curr. Opin. Struct. Biol. 2013, 23:261-267. 10.1016/j.sbi.2013.02.003.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 261-267
    • Briggs, J.A.G.1
  • 5
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic V., Forster F., Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 2005, 74:833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 8
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai X.C., Fernández I.S., McMullan G., Scheres S.H., Kuhlbrandt W. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. eLife 2013, 2. 10.7554/eLife.00461.
    • (2013) eLife , vol.2
    • Bai, X.C.1    Fernández, I.S.2    McMullan, G.3    Scheres, S.H.4    Kuhlbrandt, W.5
  • 9
    • 84866284504 scopus 로고    scopus 로고
    • Molecular basis for specific regulation of neuronal kinesin-3 motors by doublecortin family proteins
    • Liu J.S., Schubert C.R., Fu X., Fourniol F.J., Jaiswal J.K., Houdusse A., et al. Molecular basis for specific regulation of neuronal kinesin-3 motors by doublecortin family proteins. Mol. Cell 2012, 47:707-721. 10.1016/j.molcel.2012.06.025.
    • (2012) Mol. Cell , vol.47 , pp. 707-721
    • Liu, J.S.1    Schubert, C.R.2    Fu, X.3    Fourniol, F.J.4    Jaiswal, J.K.5    Houdusse, A.6
  • 11
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 1990, 213:899-929. 10.1016/S0022-2836(05)80271-2.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 12
    • 83755207591 scopus 로고    scopus 로고
    • Structural analysis of macromolecular assemblies by electron microscopy
    • Orlova E.V., Saibil H.R. Structural analysis of macromolecular assemblies by electron microscopy. Chem. Rev. 2011, 111:7710-7748.
    • (2011) Chem. Rev. , vol.111 , pp. 7710-7748
    • Orlova, E.V.1    Saibil, H.R.2
  • 13
    • 84940608127 scopus 로고    scopus 로고
    • ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space
    • Chari A., Haselbach D., Kirves J.-M., Ohmer J., Paknia E., Fischer N., et al. ProteoPlex: stability optimization of macromolecular complexes by sparse-matrix screening of chemical space. Nat. Methods 2015, 12:859-865. 10.1038/nmeth.3493.
    • (2015) Nat. Methods , vol.12 , pp. 859-865
    • Chari, A.1    Haselbach, D.2    Kirves, J.-M.3    Ohmer, J.4    Paknia, E.5    Fischer, N.6
  • 14
    • 77957239250 scopus 로고    scopus 로고
    • GraFix: stabilization of fragile macromolecular complexes for single particle cryo-EM
    • Stark H. GraFix: stabilization of fragile macromolecular complexes for single particle cryo-EM. Meth. Enzymol. 2010, 481:109-126. 10.1016/S0076-6879(10)81005-5.
    • (2010) Meth. Enzymol. , vol.481 , pp. 109-126
    • Stark, H.1
  • 15
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • Vedadi M., Niesen F.H., Allali-Hassani A., Fedorov O.Y., Finerty P.J., Wasney G.A., et al. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:15835-15840. 10.1073/pnas.0605224103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3    Fedorov, O.Y.4    Finerty, P.J.5    Wasney, G.A.6
  • 16
    • 84903310310 scopus 로고    scopus 로고
    • Structure of the mammalian ribosome-Sec61 complex to 3.4 angstrom resolution
    • Voorhees R.M., Fernández I.S., Scheres S.H.W., Hegde R.S. Structure of the mammalian ribosome-Sec61 complex to 3.4 angstrom resolution. Cell 2014, 157:1632-1643. 10.1016/j.cell.2014.05.024.
    • (2014) Cell , vol.157 , pp. 1632-1643
    • Voorhees, R.M.1    Fernández, I.S.2    Scheres, S.H.W.3    Hegde, R.S.4
  • 17
    • 84929335211 scopus 로고    scopus 로고
    • Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
    • Zhao J., Benlekbir S., Rubinstein J.L. Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase. Nature 2015.
    • (2015) Nature
    • Zhao, J.1    Benlekbir, S.2    Rubinstein, J.L.3
  • 18
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner S., Horne R.W. A negative staining method for high resolution electron microscopy of viruses. Biochim. Biophys. Acta 1959, 34:103-110. 10.1016/0006-3002(59)90237-9.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 103-110
    • Brenner, S.1    Horne, R.W.2
  • 19
    • 84857136184 scopus 로고    scopus 로고
    • Visualizing proteins and macromolecular complexes by negative stain EM: from grid preparation to image acquisition
    • Booth D.S., Avila-Sakar A., Cheng Y. Visualizing proteins and macromolecular complexes by negative stain EM: from grid preparation to image acquisition. J. Vis. Exp. 2011, 10.3791/3227.
    • (2011) J. Vis. Exp.
    • Booth, D.S.1    Avila-Sakar, A.2    Cheng, Y.3
  • 21
    • 84879724341 scopus 로고    scopus 로고
    • The respiratory syncytial virus nucleoprotein-RNA complex forms a left-handed helical nucleocapsid
    • Bakker S.E., Duquerroy S., Galloux M., Loney C., Conner E., Eleouet J.-F., et al. The respiratory syncytial virus nucleoprotein-RNA complex forms a left-handed helical nucleocapsid. J. Gen. Virol. 2013, 94:1734-1738. 10.1099/vir.0.053025-0.
    • (2013) J. Gen. Virol. , vol.94 , pp. 1734-1738
    • Bakker, S.E.1    Duquerroy, S.2    Galloux, M.3    Loney, C.4    Conner, E.5    Eleouet, J.-F.6
  • 22
    • 84902129088 scopus 로고    scopus 로고
    • PA1b inhibitor binding to subunits c and e of the Vacuolar ATPase reveals its insecticidal mechanism
    • Muench S.P., Rawson S., Eyraud V., Delmas A.F., Da Silva P., Phillips C., et al. PA1b inhibitor binding to subunits c and e of the Vacuolar ATPase reveals its insecticidal mechanism. J. Biol. Chem. 2014.
    • (2014) J. Biol. Chem.
    • Muench, S.P.1    Rawson, S.2    Eyraud, V.3    Delmas, A.F.4    Da Silva, P.5    Phillips, C.6
  • 23
    • 84925240138 scopus 로고    scopus 로고
    • DNA induces conformational changes in a recombinant human minichromosome maintenance complex
    • Hesketh E.L., Parker-Manuel R.P., Chaban Y., Satti R., Coverley D., Orlova E.V., et al. DNA induces conformational changes in a recombinant human minichromosome maintenance complex. J. Biol. Chem. 2015, 290:7973-7979. 10.1074/jbc.M114.622738.
    • (2015) J. Biol. Chem. , vol.290 , pp. 7973-7979
    • Hesketh, E.L.1    Parker-Manuel, R.P.2    Chaban, Y.3    Satti, R.4    Coverley, D.5    Orlova, E.V.6
  • 24
    • 59049095230 scopus 로고    scopus 로고
    • AAA+ ring and linker swing mechanism in the dynein motor
    • Roberts A.J., Numata N., Walker M.L., Kato Y.S., Malkova B., Kon T., et al. AAA+ ring and linker swing mechanism in the dynein motor. Cell 2009, 136:485-495. 10.1016/j.cell.2008.11.049.
    • (2009) Cell , vol.136 , pp. 485-495
    • Roberts, A.J.1    Numata, N.2    Walker, M.L.3    Kato, Y.S.4    Malkova, B.5    Kon, T.6
  • 25
    • 84859405812 scopus 로고    scopus 로고
    • Fabs enable single particle cryoEM studies of small proteins
    • Wu S., Avila-Sakar A., Kim J., Booth D.S., Greenberg C.H., Rossi A., et al. Fabs enable single particle cryoEM studies of small proteins. Structure 2012, 20:582-592. 10.1016/j.str.2012.02.017.
    • (2012) Structure , vol.20 , pp. 582-592
    • Wu, S.1    Avila-Sakar, A.2    Kim, J.3    Booth, D.S.4    Greenberg, C.H.5    Rossi, A.6
  • 26
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • Rasmussen S.G.F., DeVree B.T., Zou Y., Kruse A.C., Chung K.Y., Kobilka T.S., et al. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature 2011, 477:549-555. 10.1038/nature10361.
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.F.1    DeVree, B.T.2    Zou, Y.3    Kruse, A.C.4    Chung, K.Y.5    Kobilka, T.S.6
  • 28
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - powerful tools in modern electron microscopy
    • Ohi M., Li Y., Cheng Y., Walz T. Negative staining and image classification - powerful tools in modern electron microscopy. Biol. Proced. Online 2004, 6:23-34. 10.1251/bpo70.
    • (2004) Biol. Proced. Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 29
    • 77957232411 scopus 로고    scopus 로고
    • Cryonegative staining of macromolecular assemblies
    • De Carlo S., Stark H. Cryonegative staining of macromolecular assemblies. Methods Enzymol. 2010, 481:127-145. 10.1016/S0076-6879(10)81006-7.
    • (2010) Methods Enzymol. , vol.481 , pp. 127-145
    • De Carlo, S.1    Stark, H.2
  • 30
    • 77957222044 scopus 로고    scopus 로고
    • Radiation damage in electron cryomicroscopy
    • Baker L.A., Rubinstein J.L. Radiation damage in electron cryomicroscopy. Methods Enzymol. 2010, 481:371-388. 10.1016/S0076-6879(10)81015-8.
    • (2010) Methods Enzymol. , vol.481 , pp. 371-388
    • Baker, L.A.1    Rubinstein, J.L.2
  • 32
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 angstrom 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.S., et al. 2.2 angstrom resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor. Science 2015, 348:1147-1151. 10.1126/science.aab1576.
    • (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.S.6
  • 33
    • 84924617498 scopus 로고    scopus 로고
    • 2.8 angstrom resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy
    • Campbell M.G., Veesler D., Cheng A., Potter C.S., Carragher B. 2.8 angstrom resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy. eLife 2015, 4. 10.7554/eLife.06380.
    • (2015) eLife , vol.4
    • Campbell, M.G.1    Veesler, D.2    Cheng, A.3    Potter, C.S.4    Carragher, B.5
  • 34
    • 84897000286 scopus 로고    scopus 로고
    • The resolution revolution
    • Kuehlbrandt W. The resolution revolution. Science 2014, 343:1443-1444. 10.1126/science.1251652.
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kuehlbrandt, W.1
  • 35
    • 84944748927 scopus 로고    scopus 로고
    • Structural and biochemical basis for induced self-propagation of NLRC4
    • Hu Z., Zhou Q., Zhang C., Fan S., Cheng W., Zhao Y., et al. Structural and biochemical basis for induced self-propagation of NLRC4. Science (New York, N.Y.) 2015, 350:399-404. 10.1126/science.aac5489.
    • (2015) Science (New York, N.Y.) , vol.350 , pp. 399-404
    • Hu, Z.1    Zhou, Q.2    Zhang, C.3    Fan, S.4    Cheng, W.5    Zhao, Y.6
  • 36
    • 84949675510 scopus 로고    scopus 로고
    • Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM
    • Hesketh E.L., Meshcheriakova Y., Dent K.C., Saxena P., Thompson R.F., Cockburn J.J., et al. Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM. Nat. Commun. 2015, 6:10113. 10.1038/ncomms10113.
    • (2015) Nat. Commun. , vol.6 , pp. 10113
    • Hesketh, E.L.1    Meshcheriakova, Y.2    Dent, K.C.3    Saxena, P.4    Thompson, R.F.5    Cockburn, J.J.6
  • 37
    • 52149100074 scopus 로고    scopus 로고
    • An improved cryogen for plunge freezing
    • Tivol W.F., Briegel A., Jensen G.J. An improved cryogen for plunge freezing. Microsc. Microanal. 2008, 14:375-379. 10.1017/S1431927608080781.
    • (2008) Microsc. Microanal. , vol.14 , pp. 375-379
    • Tivol, W.F.1    Briegel, A.2    Jensen, G.J.3
  • 39
    • 33748555841 scopus 로고    scopus 로고
    • High-pressure freezing, cellular tomography, and structural cell biology
    • McDonald K.L., Auer M. High-pressure freezing, cellular tomography, and structural cell biology. Biotechniques 2006.
    • (2006) Biotechniques
    • McDonald, K.L.1    Auer, M.2
  • 40
    • 4444279375 scopus 로고    scopus 로고
    • Cryo-electron microscopy of vitreous sections of native biological cells and tissues
    • Al-Amoudi A., Norlen L., Dubochet J. Cryo-electron microscopy of vitreous sections of native biological cells and tissues. J. Struct. Biol. 2004, 148:131-135. 10.1016/j.jsb.2004.03.010.
    • (2004) J. Struct. Biol. , vol.148 , pp. 131-135
    • Al-Amoudi, A.1    Norlen, L.2    Dubochet, J.3
  • 42
    • 84934440935 scopus 로고    scopus 로고
    • Cryo-electron microscopy of vitreous sections
    • Chlanda P., Sachse M. Cryo-electron microscopy of vitreous sections. Methods Mol. Biol. 2014, 1117:193-214. 10.1007/978-1-62703-776-1_10.
    • (2014) Methods Mol. Biol. , vol.1117 , pp. 193-214
    • Chlanda, P.1    Sachse, M.2
  • 43
    • 0036440834 scopus 로고    scopus 로고
    • Freeze substitution of high-pressure frozen samples: the visibility of biological membranes is improved when the substitution medium contains water
    • Walther P., Ziegler A. Freeze substitution of high-pressure frozen samples: the visibility of biological membranes is improved when the substitution medium contains water. J. Microsc. 2002, 208:3-10. 10.1046/j.1365-2818.2002.01064.x.
    • (2002) J. Microsc. , vol.208 , pp. 3-10
    • Walther, P.1    Ziegler, A.2
  • 44
    • 27744497309 scopus 로고    scopus 로고
    • Epoxy resin as fixative during freeze-substitution
    • Matsko N., Mueller M. Epoxy resin as fixative during freeze-substitution. J. Struct. Biol. 2005, 152:92-103. 10.1016/j.jsb.2005.07.005.
    • (2005) J. Struct. Biol. , vol.152 , pp. 92-103
    • Matsko, N.1    Mueller, M.2
  • 45
    • 84887217067 scopus 로고    scopus 로고
    • Cryo FIB-SEM: volume imaging of cellular ultrastructure in native frozen specimens
    • Schertel A., Snaidero N., Han H.-M., Ruhwedel T., Laue M., Grabenbauer M., et al. Cryo FIB-SEM: volume imaging of cellular ultrastructure in native frozen specimens. J. Struct. Biol. 2013, 184:355-360. 10.1016/j.jsb.2013.09.024.
    • (2013) J. Struct. Biol. , vol.184 , pp. 355-360
    • Schertel, A.1    Snaidero, N.2    Han, H.-M.3    Ruhwedel, T.4    Laue, M.5    Grabenbauer, M.6
  • 46
    • 84867910247 scopus 로고    scopus 로고
    • 3D structure determination of native mammalian cells using cryo-FIB and cryo-electron tomography
    • Wang K., Strunk K., Zhao G., Gray J.L., Zhang P. 3D structure determination of native mammalian cells using cryo-FIB and cryo-electron tomography. J. Struct. Biol. 2012, 180:318-326. 10.1016/j.jsb.2012.07.003.
    • (2012) J. Struct. Biol. , vol.180 , pp. 318-326
    • Wang, K.1    Strunk, K.2    Zhao, G.3    Gray, J.L.4    Zhang, P.5
  • 47
    • 84939269331 scopus 로고    scopus 로고
    • Cryo-focused-ion-beam applications in structural biology
    • Rigort A., Plitzko J.M. Cryo-focused-ion-beam applications in structural biology. Arch. Biochem. Biophys. 2015, 581:122-130. 10.1016/j.abb.2015.02.009.
    • (2015) Arch. Biochem. Biophys. , vol.581 , pp. 122-130
    • Rigort, A.1    Plitzko, J.M.2
  • 48
    • 33744808536 scopus 로고    scopus 로고
    • Focused ion beam milling of vitreous water: prospects for an alternative to cryo-ultramicrotomy of frozen-hydrated biological samples
    • Marko M., Hsieh C., Moberlychan W., Mannella C.A., Frank J. Focused ion beam milling of vitreous water: prospects for an alternative to cryo-ultramicrotomy of frozen-hydrated biological samples. J. Microsc. 2006, 222:42-47. 10.1111/j.1365-2818.2006.01567.x.
    • (2006) J. Microsc. , vol.222 , pp. 42-47
    • Marko, M.1    Hsieh, C.2    Moberlychan, W.3    Mannella, C.A.4    Frank, J.5
  • 49
    • 84885847209 scopus 로고    scopus 로고
    • Opening windows into the cell: focused-ion-beam milling for cryo-electron tomography
    • Villa E., Schaffer M., Plitzko J.M., Baumeister W. Opening windows into the cell: focused-ion-beam milling for cryo-electron tomography. Curr. Opin. Struct. Biol. 2013, 23:771-777. 10.1016/j.sbi.2013.08.006.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 771-777
    • Villa, E.1    Schaffer, M.2    Plitzko, J.M.3    Baumeister, W.4
  • 50
    • 12844266145 scopus 로고    scopus 로고
    • The use of a SEM/FIB dual beam applied to biological samples
    • Mulders H. The use of a SEM/FIB dual beam applied to biological samples. GIT Imaging Microsc 2003.
    • (2003) GIT Imaging Microsc
    • Mulders, H.1
  • 51
    • 84864386261 scopus 로고    scopus 로고
    • Integrative approaches for cellular cryo-electron tomography: correlative imaging and focused ion beam micromachining
    • Rigort A., Villa E., Bäuerlein F.J.B., Engel B.D., Plitzko J.M. Integrative approaches for cellular cryo-electron tomography: correlative imaging and focused ion beam micromachining. Methods Cell Biol. 2012, 111:259-281. 10.1016/B978-0-12-416026-2.00014-5.
    • (2012) Methods Cell Biol. , vol.111 , pp. 259-281
    • Rigort, A.1    Villa, E.2    Bäuerlein, F.J.B.3    Engel, B.D.4    Plitzko, J.M.5
  • 52
    • 39149091041 scopus 로고    scopus 로고
    • Preparation of macromolecular complexes for cryo-electron microscopy
    • Grassucci R.A., Taylor D.J., Frank J. Preparation of macromolecular complexes for cryo-electron microscopy. Nat. Protoc. 2007, 2:3239-3246. 10.1038/nprot.2007.452.
    • (2007) Nat. Protoc. , vol.2 , pp. 3239-3246
    • Grassucci, R.A.1    Taylor, D.J.2    Frank, J.3
  • 53
    • 84875050513 scopus 로고    scopus 로고
    • A method to achieve homogeneous dispersion of large transmembrane complexes within the holes of carbon films for electron cryomicroscopy
    • Cheung M., Kajimura N., Makino F., Ashihara M., Miyata T., Kato T., et al. A method to achieve homogeneous dispersion of large transmembrane complexes within the holes of carbon films for electron cryomicroscopy. J. Struct. Biol. 2013, 182:51-56. 10.1016/j.jsb.2013.01.004.
    • (2013) J. Struct. Biol. , vol.182 , pp. 51-56
    • Cheung, M.1    Kajimura, N.2    Makino, F.3    Ashihara, M.4    Miyata, T.5    Kato, T.6
  • 54
    • 84917709175 scopus 로고    scopus 로고
    • Electron microscopy. Ultrastable gold substrates for electron cryomicroscopy
    • Russo C.J., Passmore L.A. Electron microscopy. Ultrastable gold substrates for electron cryomicroscopy. Science (New York, N.Y.) 2014, 346:1377-1380. 10.1126/science.1259530.
    • (2014) Science (New York, N.Y.) , vol.346 , pp. 1377-1380
    • Russo, C.J.1    Passmore, L.A.2
  • 55
    • 77952507558 scopus 로고    scopus 로고
    • Cryomesh: a new substrate for cryo-electron microscopy
    • Yoshioka C., Carragher B., Potter C.S. Cryomesh: a new substrate for cryo-electron microscopy. Microsc. Microanal. 2010, 16:43-53. 10.1017/S1431927609991310.
    • (2010) Microsc. Microanal. , vol.16 , pp. 43-53
    • Yoshioka, C.1    Carragher, B.2    Potter, C.S.3
  • 56
    • 84903542912 scopus 로고    scopus 로고
    • Controlling protein adsorption on graphene for cryo-EM using low-energy hydrogen plasmas
    • Russo C.J., Passmore L.A. Controlling protein adsorption on graphene for cryo-EM using low-energy hydrogen plasmas. Nat. Methods 2014, 10.1038/nmeth.2931.
    • (2014) Nat. Methods
    • Russo, C.J.1    Passmore, L.A.2
  • 57
    • 84954266695 scopus 로고    scopus 로고
    • Ultrastable gold substrates: properties of a support for high-resolution electron cryomicroscopy of biological specimens
    • Russo C.J., Passmore L.A. Ultrastable gold substrates: properties of a support for high-resolution electron cryomicroscopy of biological specimens. J. Struct. Biol. 2016, 193:33-44. 10.1016/j.jsb.2015.11.006.
    • (2016) J. Struct. Biol. , vol.193 , pp. 33-44
    • Russo, C.J.1    Passmore, L.A.2
  • 59
    • 84908056429 scopus 로고    scopus 로고
    • Comparison of optimal performance at 300 keV of three direct electron detectors for use in low dose electron microscopy
    • McMullan G., Faruqi A.R., Clare D., Henderson R. Comparison of optimal performance at 300 keV of three direct electron detectors for use in low dose electron microscopy. Ultramicroscopy 2014, 147:156-163. 10.1010/j.ultramic.2014.08.002.
    • (2014) Ultramicroscopy , vol.147 , pp. 156-163
    • McMullan, G.1    Faruqi, A.R.2    Clare, D.3    Henderson, R.4
  • 60
    • 77649336015 scopus 로고    scopus 로고
    • Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics
    • Cheng L., Zhu J., Hui W.H., Zhang X., Honig B., Fang Q., et al. Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics. J. Mol. Biol. 2010, 397:852-863. 10.1016/j.jmb.2009.12.027.
    • (2010) J. Mol. Biol. , vol.397 , pp. 852-863
    • Cheng, L.1    Zhu, J.2    Hui, W.H.3    Zhang, X.4    Honig, B.5    Fang, Q.6
  • 61
    • 84923368907 scopus 로고    scopus 로고
    • How cryo-EM is revolutionizing structural biology
    • Bai X.-C., McMullan G., Scheres S.H.W. How cryo-EM is revolutionizing structural biology. Trends Biochem. Sci. 2015, 40:49-57. 10.1016/j.tibs.2014.10.005.
    • (2015) Trends Biochem. Sci. , vol.40 , pp. 49-57
    • Bai, X.-C.1    McMullan, G.2    Scheres, S.H.W.3
  • 62
    • 67650538546 scopus 로고    scopus 로고
    • Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector
    • McMullan G., Faruqi A.R., Henderson R., Guerrini N., Turchetta R., Jacobs A., et al. Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector. Ultramicroscopy 2009, 109:1144-1147. 10.1016/j.ultramic.2009.05.005.
    • (2009) Ultramicroscopy , vol.109 , pp. 1144-1147
    • McMullan, G.1    Faruqi, A.R.2    Henderson, R.3    Guerrini, N.4    Turchetta, R.5    Jacobs, A.6
  • 63
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li X., Mooney P., Zheng S., Booth C.R., Braunfeld M.B., Gubbens S., et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 2013, 10:584-590. 10.1038/nmeth.2472.
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6
  • 64
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres S.H. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 2014, 3. 10.7554/eLife.03665.
    • (2014) eLife , vol.3
    • Scheres, S.H.1
  • 65
    • 84946473054 scopus 로고    scopus 로고
    • Alignment of cryo-EM movies of individual particles by optimization of image translations
    • Rubinstein J.L., Brubaker M.A. Alignment of cryo-EM movies of individual particles by optimization of image translations. J. Struct. Biol. 2015, 10.1016/j.jsb.2015.08.007.
    • (2015) J. Struct. Biol.
    • Rubinstein, J.L.1    Brubaker, M.A.2
  • 66
    • 84904461526 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain
    • Parent K.N., Tang J., Cardone G., Gilcrease E.B., Janssen M.E., Olson N.H., et al. Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain. Virology 2014, 464:55-66. 10.1016/j.virol.2014.06.017.
    • (2014) Virology , vol.464 , pp. 55-66
    • Parent, K.N.1    Tang, J.2    Cardone, G.3    Gilcrease, E.B.4    Janssen, M.E.5    Olson, N.H.6
  • 67
    • 84904560883 scopus 로고    scopus 로고
    • Three-dimensional structure of human gamma-secretase
    • Lu P., Bai X.-C., Ma D., Xie T., Yan C., Sun L., et al. Three-dimensional structure of human gamma-secretase. Nature 2014, 512:166. 10.1038/nature13567.
    • (2014) Nature , vol.512 , pp. 166
    • Lu, P.1    Bai, X.-C.2    Ma, D.3    Xie, T.4    Yan, C.5    Sun, L.6
  • 68
    • 0034903709 scopus 로고    scopus 로고
    • Transmission electron microscopy with Zernike phase plate
    • Danev R., Nagayama K. Transmission electron microscopy with Zernike phase plate. Ultramicroscopy 2001, 88:243-252. 10.1016/S0304-3991(01)00088-2.
    • (2001) Ultramicroscopy , vol.88 , pp. 243-252
    • Danev, R.1    Nagayama, K.2
  • 69
    • 80051827186 scopus 로고    scopus 로고
    • Optimizing the phase shift and the cut-on periodicity of phase plates for TEM
    • Danev R., Nagayama K. Optimizing the phase shift and the cut-on periodicity of phase plates for TEM. Ultramicroscopy 2011, 111:1305-1315. 10.1016/j.ultramic.2011.04.004.
    • (2011) Ultramicroscopy , vol.111 , pp. 1305-1315
    • Danev, R.1    Nagayama, K.2
  • 71
    • 77955481741 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions
    • Murata K., Liu X., Danev R., Jakana J., Schmid M.F., King J., et al. Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure 2010, 18:903-912. 10.1016/j.str.2010.06.006.
    • (2010) Structure , vol.18 , pp. 903-912
    • Murata, K.1    Liu, X.2    Danev, R.3    Jakana, J.4    Schmid, M.F.5    King, J.6
  • 72
    • 73449119968 scopus 로고    scopus 로고
    • Zernike phase plate cryoelectron microscopy facilitates single particle analysis of unstained asymmetric protein complexes
    • Chang W.-H., Chiu M.T.K., Chen C.-Y., Yen C.-F., Lin Y.-C., Weng Y.-P., et al. Zernike phase plate cryoelectron microscopy facilitates single particle analysis of unstained asymmetric protein complexes. Structure 2010, 18:17-27. 10.1016/j.str.2009.12.001.
    • (2010) Structure , vol.18 , pp. 17-27
    • Chang, W.-H.1    Chiu, M.T.K.2    Chen, C.-Y.3    Yen, C.-F.4    Lin, Y.-C.5    Weng, Y.-P.6
  • 74
    • 33748775731 scopus 로고    scopus 로고
    • Automated cryoEM data acquisition and analysis of 284742 particles of GroEL
    • Stagg S.M., Lander G.C., Pulokas J., Fellmann D., Cheng A., Quispe J.D., et al. Automated cryoEM data acquisition and analysis of 284742 particles of GroEL. J. Struct. Biol. 2006, 155:470-481. 10.1016/j.jsb.2006.04.005.
    • (2006) J. Struct. Biol. , vol.155 , pp. 470-481
    • Stagg, S.M.1    Lander, G.C.2    Pulokas, J.3    Fellmann, D.4    Cheng, A.5    Quispe, J.D.6
  • 75
    • 84898807479 scopus 로고    scopus 로고
    • Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
    • Unverdorben P., Beck F., Śledź P., Schweitzer A., Pfeifer G., Plitzko J.M., et al. Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome. Proc. Natl. Acad. Sci. 2014, 111:5544-5549. 10.1073/pnas.1403409111.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , pp. 5544-5549
    • Unverdorben, P.1    Beck, F.2    Śledź, P.3    Schweitzer, A.4    Pfeifer, G.5    Plitzko, J.M.6
  • 76
    • 79960898027 scopus 로고    scopus 로고
    • Computer controlled cryo-electron microscopy-TOM2 a software package for high-throughput applications
    • Korinek A., Beck F., Baumeister W., Nickell S., Plitzko J.M. Computer controlled cryo-electron microscopy-TOM2 a software package for high-throughput applications. J. Struct. Biol. 2011, 175:394-405. 10.1016/j.jsb.2011.06.003.
    • (2011) J. Struct. Biol. , vol.175 , pp. 394-405
    • Korinek, A.1    Beck, F.2    Baumeister, W.3    Nickell, S.4    Plitzko, J.M.5
  • 77
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 2005, 152:36-51. 10.1016/j.jsb.2005.07.007.
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 78
    • 77957231408 scopus 로고    scopus 로고
    • Automated data collection for electron microscopic tomography
    • Zheng S.Q., Sedat J.W., Agard D.A. Automated data collection for electron microscopic tomography. Methods Enzymol. 2010, 481:283-315. 10.1016/S0076-6879(10)81012-2.
    • (2010) Methods Enzymol. , vol.481 , pp. 283-315
    • Zheng, S.Q.1    Sedat, J.W.2    Agard, D.A.3
  • 79
  • 80
    • 60649103238 scopus 로고    scopus 로고
    • Appion: an integrated, database-driven pipeline to facilitate EM image processing
    • Lander G.C., Stagg S.M., Voss N.R., Cheng A., Fellmann D., Pulokas J., et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. J. Struct. Biol. 2009, 166:95-102. 10.1016/j.jsb.2009.01.002.
    • (2009) J. Struct. Biol. , vol.166 , pp. 95-102
    • Lander, G.C.1    Stagg, S.M.2    Voss, N.R.3    Cheng, A.4    Fellmann, D.5    Pulokas, J.6
  • 81
    • 84941242227 scopus 로고    scopus 로고
    • The revolution will not be crystallized: a new method sweeps through structural biology
    • Callaway E. The revolution will not be crystallized: a new method sweeps through structural biology. Nature 2015, 525:172-174. 10.1038/525172a.
    • (2015) Nature , vol.525 , pp. 172-174
    • Callaway, E.1
  • 83
    • 84918814424 scopus 로고    scopus 로고
    • Application of in situ diffraction in high-throughput structure determination platforms
    • Aller P., Sanchez-Weatherby J., Foadi J., Winter G., Lobley C.M.C., Axford D., et al. Application of in situ diffraction in high-throughput structure determination platforms. Methods Mol. Biol. 2015, 1261:233-253. 10.1007/978-1-4939-2230-7_13.
    • (2015) Methods Mol. Biol. , vol.1261 , pp. 233-253
    • Aller, P.1    Sanchez-Weatherby, J.2    Foadi, J.3    Winter, G.4    Lobley, C.M.C.5    Axford, D.6
  • 84
    • 84926520440 scopus 로고    scopus 로고
    • Atomic-accuracy models from 4.5-A cryo-electron microscopy data with density-guided iterative local refinement
    • DiMaio F., Song Y., Li X., Brunner M.J., Xu C., Conticello V., et al. Atomic-accuracy models from 4.5-A cryo-electron microscopy data with density-guided iterative local refinement. Nat. Methods 2015, 12:361-365. 10.1038/nmeth.3286.
    • (2015) Nat. Methods , vol.12 , pp. 361-365
    • DiMaio, F.1    Song, Y.2    Li, X.3    Brunner, M.J.4    Xu, C.5    Conticello, V.6
  • 85
    • 84855255301 scopus 로고    scopus 로고
    • Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons
    • Ibiricu I., Huiskonen J.T., Döhner K., Bradke F., Sodeik B., Grünewald K. Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons. PLoS Pathog. 2011, 7:e1002406. 10.1371/journal.ppat.1002406.
    • (2011) PLoS Pathog. , vol.7 , pp. e1002406
    • Ibiricu, I.1    Huiskonen, J.T.2    Döhner, K.3    Bradke, F.4    Sodeik, B.5    Grünewald, K.6
  • 86
    • 84857616757 scopus 로고    scopus 로고
    • Electron tomography of cells
    • Gan L., Jensen G.J. Electron tomography of cells. Q. Rev. Biophys. 2012, 45:27-56. 10.1017/S0033583511000102.
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 27-56
    • Gan, L.1    Jensen, G.J.2
  • 87
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 1998, 67:509-544. 10.1146/annurev.biochem.67.1.509.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 88
    • 84903597292 scopus 로고    scopus 로고
    • Correlated cryogenic photoactivated localization microscopy and cryo-electron tomography
    • Chang Y.W., Chen S., Tocheva E.I., Treuner-Lange A., Loebach S., Sogaard-Andersen L., et al. Correlated cryogenic photoactivated localization microscopy and cryo-electron tomography. Nat. Methods 2014, 11:737-739. 10.1038/NMETH.2961.
    • (2014) Nat. Methods , vol.11 , pp. 737-739
    • Chang, Y.W.1    Chen, S.2    Tocheva, E.I.3    Treuner-Lange, A.4    Loebach, S.5    Sogaard-Andersen, L.6
  • 91
    • 34548472879 scopus 로고    scopus 로고
    • Cryo-fluorescence microscopy facilitates correlations between light and cryo-electron microscopy and reduces the rate of photobleaching
    • Schwartz C.L., Sarbash V.I., Ataullakhanov F.I., Mcintosh J.R., Nicastro D. Cryo-fluorescence microscopy facilitates correlations between light and cryo-electron microscopy and reduces the rate of photobleaching. J. Microsc. 2007, 227:98-109. 10.1111/j.1365-2818.2007.01794.x.
    • (2007) J. Microsc. , vol.227 , pp. 98-109
    • Schwartz, C.L.1    Sarbash, V.I.2    Ataullakhanov, F.I.3    Mcintosh, J.R.4    Nicastro, D.5
  • 92
    • 35148839574 scopus 로고    scopus 로고
    • Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography
    • Sartori A., Gatz R., Beck F., Rigort A., Baumeister W., Plitzko J.M. Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography. J. Struct. Biol. 2007, 160:135-145. 10.1016/j.jsb.2007.07.011.
    • (2007) J. Struct. Biol. , vol.160 , pp. 135-145
    • Sartori, A.1    Gatz, R.2    Beck, F.3    Rigort, A.4    Baumeister, W.5    Plitzko, J.M.6
  • 93
    • 69949083343 scopus 로고    scopus 로고
    • Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells
    • Van Driel L.F., Valentijn J.A., Valentijn K.M., Koning R.I., Koster A.J. Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells. Eur. J. Cell Biol. 2009, 88:669-684. 10.1016/j.ejcb.2009.07.002.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 669-684
    • Van Driel, L.F.1    Valentijn, J.A.2    Valentijn, K.M.3    Koning, R.I.4    Koster, A.J.5
  • 94
    • 80355131379 scopus 로고    scopus 로고
    • Low-cost cryo-light microscopy stage fabrication for correlated light/electron microscopy
    • Carlson D.B., Evans J.E. Low-cost cryo-light microscopy stage fabrication for correlated light/electron microscopy. J. Vis. Exp. 2011.
    • (2011) J. Vis. Exp.
    • Carlson, D.B.1    Evans, J.E.2
  • 95
    • 77955609366 scopus 로고    scopus 로고
    • Micromachining tools and correlative approaches for cellular cryo-electron tomography
    • Rigort A., Bäuerlein F.J.B., Leis A., Gruska M., Hoffmann C., Laugks T., et al. Micromachining tools and correlative approaches for cellular cryo-electron tomography. J. Struct. Biol. 2010, 172:169-179. 10.1016/j.jsb.2010.02.011.
    • (2010) J. Struct. Biol. , vol.172 , pp. 169-179
    • Rigort, A.1    Bäuerlein, F.J.B.2    Leis, A.3    Gruska, M.4    Hoffmann, C.5    Laugks, T.6
  • 96
    • 84900842044 scopus 로고    scopus 로고
    • High-precision correlative fluorescence and electron cryo microscopy using two independent alignment markers
    • Schellenberger P., Kaufmann R., Siebert C.A., Hagen C., Wodrich H., Grünewald K. High-precision correlative fluorescence and electron cryo microscopy using two independent alignment markers. Ultramicroscopy 2014, 143:41-51. 10.1016/j.ultramic.2013.10.011.
    • (2014) Ultramicroscopy , vol.143 , pp. 41-51
    • Schellenberger, P.1    Kaufmann, R.2    Siebert, C.A.3    Hagen, C.4    Wodrich, H.5    Grünewald, K.6
  • 97
    • 27144475807 scopus 로고    scopus 로고
    • Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots
    • Giepmans B.N.G., Deerinck T.J., Smarr B.L., Jones Y.Z., Ellisman M.H. Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. Nat. Methods 2005, 2:743-749. 10.1038/nmeth791.
    • (2005) Nat. Methods , vol.2 , pp. 743-749
    • Giepmans, B.N.G.1    Deerinck, T.J.2    Smarr, B.L.3    Jones, Y.Z.4    Ellisman, M.H.5
  • 98
    • 77955768782 scopus 로고    scopus 로고
    • The use of markers for correlative light electron microscopy
    • Brown E., Verkade P. The use of markers for correlative light electron microscopy. Protoplasma 2010, 244:91-97. 10.1007/s00709-010-0165-1.
    • (2010) Protoplasma , vol.244 , pp. 91-97
    • Brown, E.1    Verkade, P.2
  • 99
    • 20144379798 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for imaging, labelling and sensing
    • Medintz I.L., Uyeda H.T., Goldman E.R., Mattoussi H. Quantum dot bioconjugates for imaging, labelling and sensing. Nat. Mater. 2005, 4:435-446. 10.1038/nmat1390.
    • (2005) Nat. Mater. , vol.4 , pp. 435-446
    • Medintz, I.L.1    Uyeda, H.T.2    Goldman, E.R.3    Mattoussi, H.4
  • 100
    • 84902518721 scopus 로고    scopus 로고
    • Super-resolution microscopy using standard fluorescent proteins in intact cells under cryo-conditions
    • Kaufmann R., Schellenberger P., Seiradake E., Dobbie I.M., Jones E.Y., Davis I., et al. Super-resolution microscopy using standard fluorescent proteins in intact cells under cryo-conditions. Nano Lett. 2014, 14:4171-4175. 10.1021/nl501870p.
    • (2014) Nano Lett. , vol.14 , pp. 4171-4175
    • Kaufmann, R.1    Schellenberger, P.2    Seiradake, E.3    Dobbie, I.M.4    Jones, E.Y.5    Davis, I.6
  • 101
    • 0034627793 scopus 로고    scopus 로고
    • Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane
    • Polishchuk R.S., Polishchuk E.V., Marra P., Alberti S., Buccione R., Luini A., et al. Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J. Cell Biol. 2000, 148:45-58.
    • (2000) J. Cell Biol. , vol.148 , pp. 45-58
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Marra, P.3    Alberti, S.4    Buccione, R.5    Luini, A.6
  • 103
    • 56149101340 scopus 로고    scopus 로고
    • Correlative light-electron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections
    • van Rijnsoever C., Oorschot V., Klumperman J. Correlative light-electron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections. Nat. Methods 2008, 5:973-980. 10.1038/nmeth.1263.
    • (2008) Nat. Methods , vol.5 , pp. 973-980
    • van Rijnsoever, C.1    Oorschot, V.2    Klumperman, J.3
  • 104
    • 84864592255 scopus 로고    scopus 로고
    • Plasma membrane reshaping during endocytosis is revealed by time-resolved electron tomography
    • Kukulski W., Schorb M., Kaksonen M., Briggs J.A.G. Plasma membrane reshaping during endocytosis is revealed by time-resolved electron tomography. Cell 2012, 150:508-520. 10.1016/j.cell.2012.05.046.
    • (2012) Cell , vol.150 , pp. 508-520
    • Kukulski, W.1    Schorb, M.2    Kaksonen, M.3    Briggs, J.A.G.4
  • 105
    • 80855156720 scopus 로고    scopus 로고
    • Direct visualization of HIV-1 with correlative live-cell microscopy and cryo-electron tomography
    • Jun S., Ke D., Debiec K., Zhao G., Meng X., Ambrose Z., et al. Direct visualization of HIV-1 with correlative live-cell microscopy and cryo-electron tomography. Structure 2011, 19:1573-1581. 10.1016/j.str.2011.09.006.
    • (2011) Structure , vol.19 , pp. 1573-1581
    • Jun, S.1    Ke, D.2    Debiec, K.3    Zhao, G.4    Meng, X.5    Ambrose, Z.6
  • 106
    • 69949083343 scopus 로고    scopus 로고
    • Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells
    • Van Driel L.F., Valentijn J.A., Valentijn K.M., Koning R.I., Koster A.J. Tools for correlative cryo-fluorescence microscopy and cryo-electron tomography applied to whole mitochondria in human endothelial cells. Eur. J. Cell Biol. 2009, 88:669-684.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 669-684
    • Van Driel, L.F.1    Valentijn, J.A.2    Valentijn, K.M.3    Koning, R.I.4    Koster, A.J.5
  • 107
    • 84857030489 scopus 로고    scopus 로고
    • Correlative VIS-fluorescence and soft X-ray cryo-microscopy/tomography of adherent cells
    • Hagen C., Guttmann P., Klupp B., Werner S., Rehbein S., Mettenleiter T.C., et al. Correlative VIS-fluorescence and soft X-ray cryo-microscopy/tomography of adherent cells. J. Struct. Biol. 2012, 177:193-201. 10.1016/j.jsb.2011.12.012.
    • (2012) J. Struct. Biol. , vol.177 , pp. 193-201
    • Hagen, C.1    Guttmann, P.2    Klupp, B.3    Werner, S.4    Rehbein, S.5    Mettenleiter, T.C.6
  • 108
    • 84900843110 scopus 로고    scopus 로고
    • Imaging endosomes and autophagosomes in whole mammalian cells using correlative cryo-fluorescence and cryo-soft X-ray microscopy (cryo-CLXM)
    • Duke E.M., Razi M., Weston A., Guttmann P., Werner S., Henzler K., et al. Imaging endosomes and autophagosomes in whole mammalian cells using correlative cryo-fluorescence and cryo-soft X-ray microscopy (cryo-CLXM). Ultramicroscopy 2014, 143:77-87. 10.1016/j.ultramic.2013.10.006.
    • (2014) Ultramicroscopy , vol.143 , pp. 77-87
    • Duke, E.M.1    Razi, M.2    Weston, A.3    Guttmann, P.4    Werner, S.5    Henzler, K.6
  • 109
    • 84877004526 scopus 로고    scopus 로고
    • Enabling direct nanoscale observations of biological reactions with dynamic TEM
    • Evans J.E., Browning N.D. Enabling direct nanoscale observations of biological reactions with dynamic TEM. Microscopy 2013, 62:147-156. 10.1093/jmicro/dfs081.
    • (2013) Microscopy , vol.62 , pp. 147-156
    • Evans, J.E.1    Browning, N.D.2
  • 110
    • 84903973914 scopus 로고    scopus 로고
    • Initial bridges between two ribosomal subunits are formed within 9.4 ms, as studied by time-resolved cryo-EM
    • Shaikh T.R., Yassin A.S., Lu Z., Barnard D., Meng X., Lu T.-M., et al. Initial bridges between two ribosomal subunits are formed within 9.4 ms, as studied by time-resolved cryo-EM. Proc. Natl. Acad. Sci. 2014, 111:9822-9827. 10.1073/pnas.1406744111.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , pp. 9822-9827
    • Shaikh, T.R.1    Yassin, A.S.2    Lu, Z.3    Barnard, D.4    Meng, X.5    Lu, T.-M.6
  • 111
    • 0028659872 scopus 로고
    • Analysis of transient structures by cryomicroscopy combined with rapid mixing of spray droplets
    • Berriman J., Unwin N. Analysis of transient structures by cryomicroscopy combined with rapid mixing of spray droplets. Ultramicroscopy 1994, 56:241-252.
    • (1994) Ultramicroscopy , vol.56 , pp. 241-252
    • Berriman, J.1    Unwin, N.2
  • 112
    • 70350234771 scopus 로고    scopus 로고
    • Monolithic microfluidic mixing-spraying devices for time-resolved cryo-electron microscopy
    • Lu Z., Shaikh T.R., Barnard D., Meng X., Mohamed H., Yassin A., et al. Monolithic microfluidic mixing-spraying devices for time-resolved cryo-electron microscopy. J. Struct. Biol. 2009, 168:388-395. 10.1016/j.jsb.2009.08.004.
    • (2009) J. Struct. Biol. , vol.168 , pp. 388-395
    • Lu, Z.1    Shaikh, T.R.2    Barnard, D.3    Meng, X.4    Mohamed, H.5    Yassin, A.6
  • 113
    • 85016924288 scopus 로고    scopus 로고
    • Two promising future developments of cryo-EM: capturing short-lived states and mapping a continuum of states of a macromolecule
    • dfv344
    • Chen B., Frank J. Two promising future developments of cryo-EM: capturing short-lived states and mapping a continuum of states of a macromolecule. Microscopy 2015, dfv344. 10.1093/jmicro/dfv344.
    • (2015) Microscopy
    • Chen, B.1    Frank, J.2
  • 114
    • 84930661954 scopus 로고    scopus 로고
    • Low cost, high performance processing of single particle cryo-electron microscopy data in the cloud
    • Cianfrocco M.A., Leschziner A.E., Scheres S.H. Low cost, high performance processing of single particle cryo-electron microscopy data in the cloud. eLife 2015, 4. 10.7554/eLife.06664.
    • (2015) eLife , vol.4
    • Cianfrocco, M.A.1    Leschziner, A.E.2    Scheres, S.H.3
  • 115
    • 84942155961 scopus 로고    scopus 로고
    • The structure of immature virus-like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly
    • Schur F.K.M., Dick R.A., Hagen W.J.H., Vogt V.M., Briggs J.A.G. The structure of immature virus-like Rous sarcoma virus gag particles reveals a structural role for the p10 domain in assembly. J. Virol. 2015, 89:10294-10302. 10.1128/JVI.01502-15.
    • (2015) J. Virol. , vol.89 , pp. 10294-10302
    • Schur, F.K.M.1    Dick, R.A.2    Hagen, W.J.H.3    Vogt, V.M.4    Briggs, J.A.G.5
  • 116
    • 84937573115 scopus 로고    scopus 로고
    • Vesicular transport. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly
    • Dodonova S.O., Diestelkoetter-Bachert P., von Appen A., Hagen W.J.H., Beck R., Beck M., et al. Vesicular transport. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly. Science (New York, N.Y.) 2015, 349:195-198. 10.1126/science.aab1121.
    • (2015) Science (New York, N.Y.) , vol.349 , pp. 195-198
    • Dodonova, S.O.1    Diestelkoetter-Bachert, P.2    von Appen, A.3    Hagen, W.J.H.4    Beck, R.5    Beck, M.6
  • 117
    • 84923923054 scopus 로고    scopus 로고
    • Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights
    • Rawson S., Phillips C., Huss M., Tiburcy F., Wieczorek H., Trinick J., et al. Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights. Structure 2015, 23:461-471. 10.1016/j.str.2014.12.016.
    • (2015) Structure , vol.23 , pp. 461-471
    • Rawson, S.1    Phillips, C.2    Huss, M.3    Tiburcy, F.4    Wieczorek, H.5    Trinick, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.