메뉴 건너뛰기




Volumn 46, Issue , 2017, Pages 87-94

Expanding the boundaries of cryo-EM with phase plates

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; CONTRAST ENHANCEMENT; CRYOELECTRON MICROSCOPY; DEFOCUS PHASE CONTRAST; ELECTRON MICROSCOPY; ELECTRON TOMOGRAPHY; IMAGE ANALYSIS; IMAGE PROCESSING; LIFESPAN; PARTICLE SIZE; PHASE PLATE; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROCESS DEVELOPMENT; PROCESS TECHNOLOGY; REVIEW; SINGLE PARTICLE ANALYSIS; SURFACE PROPERTY; TRANSMISSION ELECTRON MICROSCOPY; HUMAN; PROCEDURES; SIGNAL NOISE RATIO;

EID: 85021392373     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2017.06.006     Document Type: Review
Times cited : (78)

References (37)
  • 1
    • 84955581565 scopus 로고    scopus 로고
    • The development of cryo-EM into a mainstream structural biology technique
    • Nogales, E., The development of cryo-EM into a mainstream structural biology technique. Nat Methods 13 (2016), 24–27.
    • (2016) Nat Methods , vol.13 , pp. 24-27
    • Nogales, E.1
  • 2
    • 84922988267 scopus 로고    scopus 로고
    • Three-Dimensional Electron Microscopy of Macromolecular Assemblies: Visualization of Biological Molecules in Their Native State
    • edn 2 Oxford University Press Oxford; New York
    • Frank, J., Three-Dimensional Electron Microscopy of Macromolecular Assemblies: Visualization of Biological Molecules in Their Native State. edn 2, 2006, Oxford University Press, Oxford; New York.
    • (2006)
    • Frank, J.1
  • 3
    • 84888613557 scopus 로고    scopus 로고
    • Invited review article: methods for imaging weak-phase objects in electron microscopy
    • Glaeser, R.M., Invited review article: methods for imaging weak-phase objects in electron microscopy. Rev Sci Instrum, 84, 2013, 111101.
    • (2013) Rev Sci Instrum , vol.84 , pp. 111101
    • Glaeser, R.M.1
  • 4
    • 84941610517 scopus 로고
    • Uber die kontraste von atomen im elektronenmikroskop
    • Boersch, H., Uber die kontraste von atomen im elektronenmikroskop. Zeit Naturforsch 2a (1947), 615–633.
    • (1947) Zeit Naturforsch , vol.2a , pp. 615-633
    • Boersch, H.1
  • 5
    • 77957225478 scopus 로고    scopus 로고
    • Phase plates for transmission electron microscopy
    • (vol 481: Cryo-Em, Part A — Sample Preparation and Data Collection)
    • Danev, R., Nagayama, K., Phase plates for transmission electron microscopy. Methods Enzymol 481 (2010), 343–369 (vol 481: Cryo-Em, Part A — Sample Preparation and Data Collection).
    • (2010) Methods Enzymol , vol.481 , pp. 343-369
    • Danev, R.1    Nagayama, K.2
  • 6
    • 0034903709 scopus 로고    scopus 로고
    • Transmission electron microscopy with Zernike phase plate
    • Danev, R., Nagayama, K., Transmission electron microscopy with Zernike phase plate. Ultramicroscopy 88 (2001), 243–252.
    • (2001) Ultramicroscopy , vol.88 , pp. 243-252
    • Danev, R.1    Nagayama, K.2
  • 7
    • 80052041441 scopus 로고    scopus 로고
    • Another 60 years in electron microscopy: development of phase-plate electron microscopy and biological applications
    • Nagayama, K., Another 60 years in electron microscopy: development of phase-plate electron microscopy and biological applications. J Electron Microsc 60 (2011), S43–S62.
    • (2011) J Electron Microsc , vol.60 , pp. S43-S62
    • Nagayama, K.1
  • 8
    • 61849092662 scopus 로고    scopus 로고
    • Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy
    • Danev, R., Glaeser, R.M., Nagayama, K., Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy. Ultramicroscopy 109 (2009), 312–325.
    • (2009) Ultramicroscopy , vol.109 , pp. 312-325
    • Danev, R.1    Glaeser, R.M.2    Nagayama, K.3
  • 9
    • 84914674933 scopus 로고    scopus 로고
    • Volta potential phase plate for in-focus phase contrast transmission electron microscopy
    • Danev, R., Buijsse, B., Khoshouei, M., Plitzko, J.M., Baumeister, W., Volta potential phase plate for in-focus phase contrast transmission electron microscopy. Proc Natl Acad Sci U S A 111 (2014), 15635–15640.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 15635-15640
    • Danev, R.1    Buijsse, B.2    Khoshouei, M.3    Plitzko, J.M.4    Baumeister, W.5
  • 10
    • 77955337464 scopus 로고    scopus 로고
    • Design of an electron microscope phase plate using a focused continuous-wave laser
    • Muller, H., Jin, J.A., Danev, R., Spence, J., Padmore, H., Glaeser, R.M., Design of an electron microscope phase plate using a focused continuous-wave laser. N J Phys, 12, 2010.
    • (2010) N J Phys , vol.12
    • Muller, H.1    Jin, J.A.2    Danev, R.3    Spence, J.4    Padmore, H.5    Glaeser, R.M.6
  • 11
    • 85019192356 scopus 로고    scopus 로고
    • Continuous 40 GW/cm$^2$ laser intensity in a near-concentric optical cavity
    • arXiv:1610.08493
    • Schwartz, O., Axelrod, J.J., Haslinger, P., Ophus, C., Glaeser, R.M., Müller, H., Continuous 40 GW/cm$^2$ laser intensity in a near-concentric optical cavity. 2016 arXiv:1610.08493.
    • (2016)
    • Schwartz, O.1    Axelrod, J.J.2    Haslinger, P.3    Ophus, C.4    Glaeser, R.M.5    Müller, H.6
  • 12
    • 84884239080 scopus 로고    scopus 로고
    • Cryo-electron tomography: the challenge of doing structural biology in situ
    • Lucic, V., Rigort, A., Baumeister, W., Cryo-electron tomography: the challenge of doing structural biology in situ. J Cell Biol 202 (2013), 407–419.
    • (2013) J Cell Biol , vol.202 , pp. 407-419
    • Lucic, V.1    Rigort, A.2    Baumeister, W.3
  • 13
    • 77953700668 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron tomography
    • Danev, R., Kanamaru, S., Marko, M., Nagayama, K., Zernike phase contrast cryo-electron tomography. J Struct Biol 171 (2010), 174–181.
    • (2010) J Struct Biol , vol.171 , pp. 174-181
    • Danev, R.1    Kanamaru, S.2    Marko, M.3    Nagayama, K.4
  • 14
    • 70350227153 scopus 로고    scopus 로고
    • Tuning of the Zernike phase-plate for visualization of detailed ultrastructure in complex biological specimens
    • Fukuda, Y., Fukazawa, Y., Danev, R., Shigemoto, R., Nagayama, K., Tuning of the Zernike phase-plate for visualization of detailed ultrastructure in complex biological specimens. J Struct Biol 168 (2009), 476–484.
    • (2009) J Struct Biol , vol.168 , pp. 476-484
    • Fukuda, Y.1    Fukazawa, Y.2    Danev, R.3    Shigemoto, R.4    Nagayama, K.5
  • 15
    • 42649085376 scopus 로고    scopus 로고
    • Zernike phase contrast electron microscopy of ice-embedded influenza A virus
    • Yamaguchi, M., Danev, R., Nishiyama, K., Sugawara, K., Nagayama, K., Zernike phase contrast electron microscopy of ice-embedded influenza A virus. J Struct Biol 162 (2008), 271–276.
    • (2008) J Struct Biol , vol.162 , pp. 271-276
    • Yamaguchi, M.1    Danev, R.2    Nishiyama, K.3    Sugawara, K.4    Nagayama, K.5
  • 16
    • 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., Nagayama, K., Chiu, W., Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure 18 (2010), 903–912.
    • (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    Nagayama, K.7    Chiu, W.8
  • 18
    • 84908192094 scopus 로고    scopus 로고
    • Zernike phase-contrast electron cryotomography applied to marine cyanobacteria infected with cyanophages
    • Dai, W., Fu, C., Khant, H.A., Ludtke, S.J., Schmid, M.F., Chiu, W., Zernike phase-contrast electron cryotomography applied to marine cyanobacteria infected with cyanophages. Nat Protoc 9 (2014), 2630–2642.
    • (2014) Nat Protoc , vol.9 , pp. 2630-2642
    • Dai, W.1    Fu, C.2    Khant, H.A.3    Ludtke, S.J.4    Schmid, M.F.5    Chiu, W.6
  • 19
    • 84928696968 scopus 로고    scopus 로고
    • Electron cryotomography of vitrified cells with a Volta phase plate
    • The authors evaluated the performance of the Volta phase plate (VPP) for cryo-electron tomography. They compared the contrast gain from the VPP with that of an energy filter.
    • 19• Fukuda, Y., Laugks, U., Lucic, V., Baumeister, W., Danev, R., Electron cryotomography of vitrified cells with a Volta phase plate. J Struct Biol 190 (2015), 143–154 The authors evaluated the performance of the Volta phase plate (VPP) for cryo-electron tomography. They compared the contrast gain from the VPP with that of an energy filter.
    • (2015) J Struct Biol , vol.190 , pp. 143-154
    • Fukuda, Y.1    Laugks, U.2    Lucic, V.3    Baumeister, W.4    Danev, R.5
  • 20
    • 84921752079 scopus 로고    scopus 로고
    • A molecular census of 26S proteasomes in intact neurons
    • This study demonstrated for the first time the capability of phase plate cryo-tomography for ‘visual proteomics’, that is, mapping of the positions and the conformational states of protein complexes in situ.
    • 20•• Asano, S., Fukuda, Y., Beck, F., Aufderheide, A., Forster, F., Danev, R., Baumeister, W., A molecular census of 26S proteasomes in intact neurons. Science 347 (2015), 439–442 This study demonstrated for the first time the capability of phase plate cryo-tomography for ‘visual proteomics’, that is, mapping of the positions and the conformational states of protein complexes in situ.
    • (2015) Science , vol.347 , pp. 439-442
    • Asano, S.1    Fukuda, Y.2    Beck, F.3    Aufderheide, A.4    Forster, F.5    Danev, R.6    Baumeister, W.7
  • 21
    • 84963538105 scopus 로고    scopus 로고
    • Heterogeneous MAC initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography
    • Sharp, T.H., Koster, A.J., Gros, P., Heterogeneous MAC initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography. Cell Rep 15 (2016), 1–8.
    • (2016) Cell Rep , vol.15 , pp. 1-8
    • Sharp, T.H.1    Koster, A.J.2    Gros, P.3
  • 23
    • 84959419478 scopus 로고    scopus 로고
    • Visualizing the molecular sociology at the HeLa cell nuclear periphery
    • Using Volta phase plate cryo-tomography the authors visualized the molecular organization around the nuclear envelope of HeLa cells in unprecedented detail.
    • 23• Mahamid, J., Pfeffer, S., Schaffer, M., Villa, E., Danev, R., Cuellar, L.K., Forster, F., Hyman, A.A., Plitzko, J.M., Baumeister, W., Visualizing the molecular sociology at the HeLa cell nuclear periphery. Science 351 (2016), 969–972 Using Volta phase plate cryo-tomography the authors visualized the molecular organization around the nuclear envelope of HeLa cells in unprecedented detail.
    • (2016) Science , vol.351 , pp. 969-972
    • Mahamid, J.1    Pfeffer, S.2    Schaffer, M.3    Villa, E.4    Danev, R.5    Cuellar, L.K.6    Forster, F.7    Hyman, A.A.8    Plitzko, J.M.9    Baumeister, W.10
  • 25
    • 85002737040 scopus 로고    scopus 로고
    • Optimized cryo-focused ion beam sample preparation aimed at in situ structural studies of membrane proteins
    • Schaffer, M., Mahamid, J., Engel, B.D., Laugks, T., Baumeister, W., Plitzko, J.M., Optimized cryo-focused ion beam sample preparation aimed at in situ structural studies of membrane proteins. J Struct Biol 197 (2017), 73–82.
    • (2017) J Struct Biol , vol.197 , pp. 73-82
    • Schaffer, M.1    Mahamid, J.2    Engel, B.D.3    Laugks, T.4    Baumeister, W.5    Plitzko, J.M.6
  • 26
    • 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 161 (2015), 438–449.
    • (2015) Cell , vol.161 , pp. 438-449
    • Cheng, Y.1    Grigorieff, N.2    Penczek, P.A.3    Walz, T.4
  • 27
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic-resolution microscopy of unstained biological molecules
    • Henderson, R., The potential and limitations of neutrons, electrons and X-rays for atomic-resolution microscopy of unstained biological molecules. Q Rev Biophys 28 (1995), 171–193.
    • (1995) Q Rev Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 28
    • 0033377941 scopus 로고    scopus 로고
    • Review: electron crystallography: present excitement, a nod to the past, anticipating the future
    • Glaeser, R.M., Review: electron crystallography: present excitement, a nod to the past, anticipating the future. J Struct Biol 128 (1999), 3–14.
    • (1999) J Struct Biol , vol.128 , pp. 3-14
    • Glaeser, R.M.1
  • 29
    • 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., Chang, J.C., Wu, Y.M., Cheng, H., Fu, J.H., et al. Zernike phase plate cryoelectron microscopy facilitates single particle analysis of unstained asymmetric protein complexes. Structure 18 (2010), 17–27.
    • (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    Chang, J.C.7    Wu, Y.M.8    Cheng, H.9    Fu, J.H.10
  • 30
    • 79955669566 scopus 로고    scopus 로고
    • Accurate modeling of single-particle cryo-EM images quantitates the benefits expected from using Zernike phase contrast
    • Hall, R.J., Nogales, E., Glaeser, R.M., Accurate modeling of single-particle cryo-EM images quantitates the benefits expected from using Zernike phase contrast. J Struct Biol 174 (2011), 468–475.
    • (2011) J Struct Biol , vol.174 , pp. 468-475
    • Hall, R.J.1    Nogales, E.2    Glaeser, R.M.3
  • 31
    • 38349081491 scopus 로고    scopus 로고
    • Single particle analysis based on Zernike phase contrast transmission electron microscopy
    • Danev, R., Nagayama, K., Single particle analysis based on Zernike phase contrast transmission electron microscopy. J Struct Biol 161 (2008), 211–218.
    • (2008) J Struct Biol , vol.161 , pp. 211-218
    • Danev, R.1    Nagayama, K.2
  • 32
    • 78951479560 scopus 로고    scopus 로고
    • Seeing the portal in herpes simplex virus type 1 B capsids
    • Rochat, R.H., Liu, X., Murata, K., Nagayama, K., Rixon, F.J., Chiu, W., Seeing the portal in herpes simplex virus type 1 B capsids. J Virol 85 (2011), 1871–1874.
    • (2011) J Virol , vol.85 , pp. 1871-1874
    • Rochat, R.H.1    Liu, X.2    Murata, K.3    Nagayama, K.4    Rixon, F.J.5    Chiu, W.6
  • 33
    • 84968725663 scopus 로고    scopus 로고
    • Cryo-EM single particle analysis with the Volta phase plate
    • Danev, R., Baumeister, W., Cryo-EM single particle analysis with the Volta phase plate. Elife, 5, 2016.
    • (2016) Elife , vol.5
    • Danev, R.1    Baumeister, W.2
  • 34
    • 85011422346 scopus 로고    scopus 로고
    • Using the Volta phase plate with defocus for cryo-EM single particle analysis
    • This work describes a single particle approach which combines the Volta phase plate with a small amount of defocus and demonstrates its ability to reach resolutions in the 2 Å range.
    • 34•• Danev, R., Tegunov, D., Baumeister, W., Using the Volta phase plate with defocus for cryo-EM single particle analysis. Elife, 2017, 6 This work describes a single particle approach which combines the Volta phase plate with a small amount of defocus and demonstrates its ability to reach resolutions in the 2 Å range.
    • (2017) Elife , pp. 6
    • Danev, R.1    Tegunov, D.2    Baumeister, W.3
  • 37
    • 85011369030 scopus 로고    scopus 로고
    • Cryo-EM structure of haemoglobin at 3.2 A determined with the Volta phase plate
    • With the help of the Volta phase plate the authors succeeded in determining the structure of hemoglobin at near-atomic resolution. Currently, this result represents the smallest protein solved to near-atomic resolution by cryo-EM single particle analysis.
    • 37• Khoshouei, M., Radjainia, M., Baumeister, W., Danev, R., Cryo-EM structure of haemoglobin at 3.2 A determined with the Volta phase plate. bioRxiv, 2016, 10.1101/087841 With the help of the Volta phase plate the authors succeeded in determining the structure of hemoglobin at near-atomic resolution. Currently, this result represents the smallest protein solved to near-atomic resolution by cryo-EM single particle analysis.
    • (2016) bioRxiv
    • Khoshouei, M.1    Radjainia, M.2    Baumeister, W.3    Danev, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.