메뉴 건너뛰기




Volumn 110, Issue 4, 2016, Pages 749-755

Factors that Influence the Formation and Stability of Thin, Cryo-EM Specimens

Author keywords

[No Author keywords available]

Indexed keywords

AIR; SOLVENT; SURFACTANT; WATER;

EID: 84959514629     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.07.050     Document Type: Review
Times cited : (65)

References (29)
  • 1
    • 0021257186 scopus 로고
    • Cryo-electron microscopy of viruses
    • M. Adrian, and J. Dubochet A.W. McDowall Cryo-electron microscopy of viruses Nature 308 1984 32 36
    • (1984) Nature , vol.308 , pp. 32-36
    • Adrian, M.1    Dubochet, J.2    McDowall, A.W.3
  • 2
    • 0001298807 scopus 로고
    • Cryo-electron microscopy of vitrified biological specimens
    • J. Dubochet, and M. Adrian A.W. McDowall Cryo-electron microscopy of vitrified biological specimens Trends Biochem. Sci. 10 1985 143 146
    • (1985) Trends Biochem. Sci. , vol.10 , pp. 143-146
    • Dubochet, J.1    Adrian, M.2    McDowall, A.W.3
  • 4
    • 84905217139 scopus 로고    scopus 로고
    • Single-particle cryo-electron microscopy (Cryo-EM): Progress, challenges, and perspectives for further improvement
    • P.W. Hawkes, Elsevier New York
    • D. Agard, and Y. Cheng S. Subramaniam Single-particle cryo-electron microscopy (Cryo-EM): progress, challenges, and perspectives for further improvement P.W. Hawkes, Advances in Imaging and Electron Physics 2014 Elsevier New York 113 137
    • (2014) Advances in Imaging and Electron Physics , pp. 113-137
    • Agard, D.1    Cheng, Y.2    Subramaniam, S.3
  • 5
    • 84930667920 scopus 로고    scopus 로고
    • 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
    • A. Bartesaghi, and A. Merk S. Subramaniam 2.2 Å resolution cryo-EM structure of β-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    Subramaniam, S.3
  • 6
    • 0035783389 scopus 로고    scopus 로고
    • Alignment error envelopes for single particle analysis
    • G.J. Jensen Alignment error envelopes for single particle analysis J. Struct. Biol. 133 2001 143 155
    • (2001) J. Struct. Biol. , vol.133 , pp. 143-155
    • Jensen, G.J.1
  • 7
    • 0003098343 scopus 로고
    • An essay on the cohesion of fluids
    • T. Young An essay on the cohesion of fluids Philos. Trans. R. Soc. Lond. 95 1805 65 87
    • (1805) Philos. Trans. R. Soc. Lond. , vol.95 , pp. 65-87
    • Young, T.1
  • 8
    • 84986676687 scopus 로고
    • Phospholipid, nature's own slide and cover slip for cryo-electron microscopy
    • P.M. Frederik, and M.C.A. Stuart W.M. Busing Phospholipid, nature's own slide and cover slip for cryo-electron microscopy J. Microsc. 153 1989 81 92
    • (1989) J. Microsc. , vol.153 , pp. 81-92
    • Frederik, P.M.1    Stuart, M.C.A.2    Busing, W.M.3
  • 11
    • 0001121186 scopus 로고
    • Drying of solids wetted by thin liquid films
    • F.B. Wyart, and J. Daillant Drying of solids wetted by thin liquid films Can. J. Phys. 68 1990 1084 1088
    • (1990) Can. J. Phys. , vol.68 , pp. 1084-1088
    • Wyart, F.B.1    Daillant, J.2
  • 12
    • 4444240383 scopus 로고
    • Possible mechanism for spontaneous rupture of thin, free liquid films
    • A. Vrij Possible mechanism for spontaneous rupture of thin, free liquid films Discuss. Faraday Soc. 42 1966 23 33
    • (1966) Discuss. Faraday Soc. , vol.42 , pp. 23-33
    • Vrij, A.1
  • 14
    • 0000843188 scopus 로고
    • How does a thin wetted film dry up?
    • M. Elbaum, and S.G. Lipson How does a thin wetted film dry up? Phys. Rev. Lett. 72 1994 3562 3565
    • (1994) Phys. Rev. Lett. , vol.72 , pp. 3562-3565
    • Elbaum, M.1    Lipson, S.G.2
  • 15
    • 84855883174 scopus 로고    scopus 로고
    • Hydration forces: Observations, explanations, expectations, questions
    • V.A. Parsegian, and T. Zemb Hydration forces: observations, explanations, expectations, questions Curr. Opin. Colloid Interface Sci. 16 2011 618 624
    • (2011) Curr. Opin. Colloid Interface Sci. , vol.16 , pp. 618-624
    • Parsegian, V.A.1    Zemb, T.2
  • 17
    • 0028964069 scopus 로고
    • Range and magnitude of the steric pressure between bilayers containing phospholipids with covalently attached poly(ethylene glycol)
    • A.K. Kenworthy, and K. Hristova T.J. McIntosh Range and magnitude of the steric pressure between bilayers containing phospholipids with covalently attached poly(ethylene glycol) Biophys. J. 68 1995 1921 1936
    • (1995) Biophys. J. , vol.68 , pp. 1921-1936
    • Kenworthy, A.K.1    Hristova, K.2    McIntosh, T.J.3
  • 18
    • 0021191386 scopus 로고
    • Preparation of frozen-hydrated specimens for high resolution electron microscopy
    • J.S. Jaffe, and R.M. Glaeser Preparation of frozen-hydrated specimens for high resolution electron microscopy Ultramicroscopy 13 1984 373 377
    • (1984) Ultramicroscopy , vol.13 , pp. 373-377
    • Jaffe, J.S.1    Glaeser, R.M.2
  • 19
    • 0015670046 scopus 로고
    • Hydrophilic support films of controlled thickness and composition
    • K.A. Taylor, and R.M. Glaeser Hydrophilic support films of controlled thickness and composition Rev. Sci. Instrum. 44 1973 1546 1547
    • (1973) Rev. Sci. Instrum. , vol.44 , pp. 1546-1547
    • Taylor, K.A.1    Glaeser, R.M.2
  • 20
    • 0021934683 scopus 로고
    • The fatty-acid monolayer technique for preparing frozen-hydrated specimens
    • C.F. Chang, T. Ohno, and R.M. Glaeser The fatty-acid monolayer technique for preparing frozen-hydrated specimens J. Electron Microsc. Tech. 2 1985 59 65
    • (1985) J. Electron Microsc. Tech. , vol.2 , pp. 59-65
    • Chang, C.F.1    Ohno, T.2    Glaeser, R.M.3
  • 21
    • 0018072802 scopus 로고
    • Molecular orientation of bacteriorhodopsin within the purple membrane of Halobacterium halobium
    • S.B. Hayward, and D.A. Grano K.A. Fisher Molecular orientation of bacteriorhodopsin within the purple membrane of Halobacterium halobium Proc. Natl. Acad. Sci. USA 75 1978 4320 4324
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4320-4324
    • Hayward, S.B.1    Grano, D.A.2    Fisher, K.A.3
  • 22
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • E. Cao, and M. Liao D. Julius TRPV1 structures in distinct conformations reveal activation mechanisms Nature 504 2013 113 118
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Julius, D.3
  • 23
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megaDalton cryo-EM particles
    • S.H. Scheres Beam-induced motion correction for sub-megaDalton cryo-EM particles eLife 3 2014 e03665
    • (2014) ELife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 24
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • X. Li, and P. Mooney Y. Cheng 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.1    Mooney, P.2    Cheng, Y.3
  • 25
    • 84924617498 scopus 로고    scopus 로고
    • 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20 S proteasome using cryo-electron microscopy
    • 03/2015; 4
    • M.G. Campbell, and D. Veesler B. Carragher 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20 S proteasome using cryo-electron microscopy eLife Sci 2015 10.7554/eLife.06380 03/2015; 4
    • (2015) ELife Sci
    • Campbell, M.G.1    Veesler, D.2    Carragher, B.3
  • 27
    • 0031647309 scopus 로고    scopus 로고
    • Wetting and capillary phenomena of water on mica
    • L. Xu, and A. Lio M. Salmeron Wetting and capillary phenomena of water on mica J. Phys. Chem. B 102 1998 540 548
    • (1998) J. Phys. Chem. B , vol.102 , pp. 540-548
    • Xu, L.1    Lio, A.2    Salmeron, M.3
  • 28
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • C. Tribet, R. Audebert, and J.L. Popot Amphipols: polymers that keep membrane proteins soluble in aqueous solutions Proc. Natl. Acad. Sci. USA 93 1996 15047 15050
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.L.3
  • 29
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • M. Liao, and E. Cao Y. Cheng 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    Cheng, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.