메뉴 건너뛰기




Volumn 42, Issue 2, 2011, Pages 186-195

Assessing the structure and function of single biomolecules with scanning transmission electron and atomic force microscopes

Author keywords

Atomic force microscopy; Force spectroscopy; High resolution imaging; Intermolecular interactions; Mass mapping; Scanning transmission electron microscopy

Indexed keywords

FORCE SPECTROSCOPY; HIGH-RESOLUTION IMAGING; INTERMOLECULAR INTERACTIONS; MASS-MAPPING; SCANNING TRANSMISSION ELECTRON MICROSCOPY;

EID: 78649857304     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micron.2010.10.002     Document Type: Review
Times cited : (25)

References (56)
  • 1
    • 5844416566 scopus 로고
    • Das Elektronen Rastermikroskop, Theoretische Grundlagen
    • von Ardenne M. Das Elektronen Rastermikroskop, Theoretische Grundlagen. Z. Physik 1938, 109:553-560.
    • (1938) Z. Physik , vol.109 , pp. 553-560
    • von Ardenne, M.1
  • 2
    • 0019549312 scopus 로고
    • The structure of the cell envelope of Micrococcus radiodurans as revealed by metal shadowing and decoration
    • Baumeister W., Kübler O., Zingsheim H.P. The structure of the cell envelope of Micrococcus radiodurans as revealed by metal shadowing and decoration. J. Ultrastruct. Res. 1981, 75:60-71.
    • (1981) J. Ultrastruct. Res. , vol.75 , pp. 60-71
    • Baumeister, W.1    Kübler, O.2    Zingsheim, H.P.3
  • 4
    • 0000006242 scopus 로고
    • Scanning tunneling microscopy
    • Binnig G., Rohrer H. Scanning tunneling microscopy. Helv. Phys. Acta 1982, 55:726-735.
    • (1982) Helv. Phys. Acta , vol.55 , pp. 726-735
    • Binnig, G.1    Rohrer, H.2
  • 5
    • 19044362545 scopus 로고
    • 7×7 Reconstruction on Si(111) resolved in real space
    • Binnig G., Rohrer H., Gerber C., Weibel E. 7×7 Reconstruction on Si(111) resolved in real space. Phys. Rev. Lett. 1983, 50:120-123.
    • (1983) Phys. Rev. Lett. , vol.50 , pp. 120-123
    • Binnig, G.1    Rohrer, H.2    Gerber, C.3    Weibel, E.4
  • 8
    • 0017689848 scopus 로고
    • Molecular microscopy of labeled polynucleotides: stability of osmium atoms
    • Cole M.D., Wiggins J.W., Beer M. Molecular microscopy of labeled polynucleotides: stability of osmium atoms. J. Mol. Biol. 1977, 117:387-400.
    • (1977) J. Mol. Biol. , vol.117 , pp. 387-400
    • Cole, M.D.1    Wiggins, J.W.2    Beer, M.3
  • 9
    • 37049250176 scopus 로고
    • Visibility of single atoms
    • Crewe A.V., Wall J., Langmore J. Visibility of single atoms. Science 1970, 168:1338-1340.
    • (1970) Science , vol.168 , pp. 1338-1340
    • Crewe, A.V.1    Wall, J.2    Langmore, J.3
  • 11
    • 0018197443 scopus 로고
    • Molecular weight determination by scanning transmission electron microscopy
    • Engel A. Molecular weight determination by scanning transmission electron microscopy. Ultramicroscopy 1978, 3:273-281.
    • (1978) Ultramicroscopy , vol.3 , pp. 273-281
    • Engel, A.1
  • 12
    • 71849110960 scopus 로고    scopus 로고
    • Scanning transmission electron microscopy: biological applications
    • Academic Press, Burlington, USA
    • Engel A. Scanning transmission electron microscopy: biological applications. Advances in Imaging and Electron Physics 2009, vol. 159:357-386. Academic Press, Burlington, USA.
    • (2009) Advances in Imaging and Electron Physics , vol.159 , pp. 357-386
    • Engel, A.1
  • 13
    • 0020158294 scopus 로고
    • Mass mapping of a protein complex with the scanning transmission electron microscope
    • Engel A., Baumeister W., Saxton W.O. Mass mapping of a protein complex with the scanning transmission electron microscope. Proc. Natl. Acad. Sci. U.S.A. 1982, 79:4050-4054.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4050-4054
    • Engel, A.1    Baumeister, W.2    Saxton, W.O.3
  • 14
    • 50649125304 scopus 로고    scopus 로고
    • Structure and mechanics of membrane proteins
    • Engel A., Gaub H.E. Structure and mechanics of membrane proteins. Annu. Rev. Biochem. 2008, 77:127-148.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 127-148
    • Engel, A.1    Gaub, H.E.2
  • 16
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • Engel A., Müller D.J. Observing single biomolecules at work with the atomic force microscope. Nat. Struct. Biol. 2000, 7:715-718.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 19
    • 0029311286 scopus 로고
    • Optimum rotationally symmetric detector configurations for phase contrast imaging in scanning transmission electron microscopy
    • Hammel M., Rose H. Optimum rotationally symmetric detector configurations for phase contrast imaging in scanning transmission electron microscopy. Ultramicroscopy 1995, 58:403-415.
    • (1995) Ultramicroscopy , vol.58 , pp. 403-415
    • Hammel, M.1    Rose, H.2
  • 23
    • 0028087275 scopus 로고
    • Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment
    • Karrasch S., Hegerl R., Hoh J., Baumeister W., Engel A. Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:836-838.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 836-838
    • Karrasch, S.1    Hegerl, R.2    Hoh, J.3    Baumeister, W.4    Engel, A.5
  • 24
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • Kedrov A., Janovjak H., Sapra K.T., Müller D.J. Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:233-260.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Müller, D.J.4
  • 25
    • 28844490188 scopus 로고    scopus 로고
    • Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli
    • Kedrov A., Janovjak H., Ziegler C., Kuhlbrandt W., Müller D.J. Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. J. Mol. Biol. 2006, 355:2-8.
    • (2006) J. Mol. Biol. , vol.355 , pp. 2-8
    • Kedrov, A.1    Janovjak, H.2    Ziegler, C.3    Kuhlbrandt, W.4    Müller, D.J.5
  • 27
    • 1542306888 scopus 로고    scopus 로고
    • Young's modulus of silicon nitride used in scanning force microscope cantilevers
    • Khan A., Hess P. Young's modulus of silicon nitride used in scanning force microscope cantilevers. J. Appl. Phys. 2004, 95:1667-17672.
    • (2004) J. Appl. Phys. , vol.95 , pp. 1667-17672
    • Khan, A.1    Hess, P.2
  • 28
    • 77950283360 scopus 로고    scopus 로고
    • Atom-by-atom structural and chemical analysis by annular dark-field electron microscopy
    • Krivanek O. Atom-by-atom structural and chemical analysis by annular dark-field electron microscopy. Nature 2010, 464:571.
    • (2010) Nature , vol.464 , pp. 571
    • Krivanek, O.1
  • 29
    • 0030029859 scopus 로고    scopus 로고
    • High resolution surface structure of E. coli GroES oligomer by atomic force microscopy
    • Mou J., Czajkowsky D.M., Sheng S., Ho R., Shao Z. High resolution surface structure of E. coli GroES oligomer by atomic force microscopy. FEBS Lett. 1996, 381:161-164.
    • (1996) FEBS Lett. , vol.381 , pp. 161-164
    • Mou, J.1    Czajkowsky, D.M.2    Sheng, S.3    Ho, R.4    Shao, Z.5
  • 30
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller D.J., Amrein M., Engel A. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 1997, 119:172-188.
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 31
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy
    • Müller D.J., Baumeister W., Engel A. Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy. J. Bacteriol. 1996, 178:3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 32
  • 33
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Müller D.J., Engel A. Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J. Mol. Biol. 1999, 285:1347-1351.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 34
    • 38449087324 scopus 로고    scopus 로고
    • Atomic force microscopy and spectroscopy of native membrane proteins
    • Müller D.J., Engel A. Atomic force microscopy and spectroscopy of native membrane proteins. Nat. Protoc. 2007, 2:2191-2197.
    • (2007) Nat. Protoc. , vol.2 , pp. 2191-2197
    • Müller, D.J.1    Engel, A.2
  • 35
    • 0039114981 scopus 로고    scopus 로고
    • Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope
    • Müller D.J., Fotiadis D., Scheuring S., Müller S.A., Engel A. Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope. Biophys. J. 1999, 76:1101-1111.
    • (1999) Biophys. J. , vol.76 , pp. 1101-1111
    • Müller, D.J.1    Fotiadis, D.2    Scheuring, S.3    Müller, S.A.4    Engel, A.5
  • 36
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated connexin 26 gap junctions
    • Müller D.J., Hand G.M., Engel A., Sosinsky G.E. Conformational changes in surface structures of isolated connexin 26 gap junctions. EMBO J. 2002, 21:3598-3607.
    • (2002) EMBO J. , vol.21 , pp. 3598-3607
    • Müller, D.J.1    Hand, G.M.2    Engel, A.3    Sosinsky, G.E.4
  • 37
    • 0031855721 scopus 로고    scopus 로고
    • Mass measurement in the scanning transmission electron microscope: a powerful tool for studying membrane proteins
    • Müller S.A., Engel A. Mass measurement in the scanning transmission electron microscope: a powerful tool for studying membrane proteins. J. Struct. Biol. 1998, 121:219-230.
    • (1998) J. Struct. Biol. , vol.121 , pp. 219-230
    • Müller, S.A.1    Engel, A.2
  • 38
    • 0035239217 scopus 로고    scopus 로고
    • Structure and mass analysis by scanning transmission electron microscopy
    • Müller S.A., Engel A. Structure and mass analysis by scanning transmission electron microscopy. Micron 2001, 32:21-31.
    • (2001) Micron , vol.32 , pp. 21-31
    • Müller, S.A.1    Engel, A.2
  • 39
    • 33845666839 scopus 로고    scopus 로고
    • Biological scanning transmission electron microscopy: imaging and single molecule mass determination
    • Müller S.A., Engel A. Biological scanning transmission electron microscopy: imaging and single molecule mass determination. Chimia 2006, 60:749-753.
    • (2006) Chimia , vol.60 , pp. 749-753
    • Müller, S.A.1    Engel, A.2
  • 40
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • Müller S.A., Goldie K.N., Buerki R., Haering R., Engel A. Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy 1992, 46:317-334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Buerki, R.3    Haering, R.4    Engel, A.5
  • 41
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E.L., Jarnik M., Engel A., Aebi U. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 1990, 110:883-894.
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 42
    • 0032109073 scopus 로고    scopus 로고
    • Frequency response of cantilever beams immersed in viscous fluids with applications to the atomic force microscope
    • Sader J.E. Frequency response of cantilever beams immersed in viscous fluids with applications to the atomic force microscope. J. Appl. Phys. 1998, 84:64-76.
    • (1998) J. Appl. Phys. , vol.84 , pp. 64-76
    • Sader, J.E.1
  • 43
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W.O., Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 1982, 127:127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 44
    • 36049012024 scopus 로고    scopus 로고
    • Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains
    • Scheuring S., Buzhynskyy N., Jaroslawski S., Goncalves R.P., Hite R.K., Walz T. Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains. J. Struct. Biol. 2007, 160:385-394.
    • (2007) J. Struct. Biol. , vol.160 , pp. 385-394
    • Scheuring, S.1    Buzhynskyy, N.2    Jaroslawski, S.3    Goncalves, R.P.4    Hite, R.K.5    Walz, T.6
  • 45
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring S., Sturgis J.N. Chromatic adaptation of photosynthetic membranes. Science 2005, 309:484-487.
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 46
    • 13444280089 scopus 로고    scopus 로고
    • How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations
    • Schiener J., Witt S., Hayer-Hartl M., Guckenberger R. How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations. Biochem. Biophys. Res. Commun. 2005, 328:477-483.
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 477-483
    • Schiener, J.1    Witt, S.2    Hayer-Hartl, M.3    Guckenberger, R.4
  • 47
    • 59649110824 scopus 로고    scopus 로고
    • Monte Carlo electron trajectory simulations in bright-field and dark-field STEM: implications for tomography of thick biological sections
    • Sousa A.A., Hohmann-Marriott M.F., Zhang G., Leapman R.D. Monte Carlo electron trajectory simulations in bright-field and dark-field STEM: implications for tomography of thick biological sections. Ultramicroscopy 2009, 109:213-221.
    • (2009) Ultramicroscopy , vol.109 , pp. 213-221
    • Sousa, A.A.1    Hohmann-Marriott, M.F.2    Zhang, G.3    Leapman, R.D.4
  • 50
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas D., Schultz P., Steven A.C., Wall J.S. Mass analysis of biological macromolecular complexes by STEM. Biol. Cell 1994, 80:181-192.
    • (1994) Biol. Cell , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3    Wall, J.S.4
  • 52
    • 0022526226 scopus 로고
    • Mass mapping with the scanning transmission electron microscope
    • Wall J.S., Hainfeld J.F. Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Chem. 1986, 15:355-376.
    • (1986) Annu. Rev. Biophys. Chem. , vol.15 , pp. 355-376
    • Wall, J.S.1    Hainfeld, J.F.2
  • 53
    • 71549135852 scopus 로고    scopus 로고
    • History of the STEM at Brookhaven National Laboratory
    • Academic Press, Burlington, USA, P. Hawkes (Ed.)
    • Wall J., Simon M., Hainfeld J. History of the STEM at Brookhaven National Laboratory. Advances in Imaging and Electron Physics 2009, 101-121. Academic Press, Burlington, USA. P. Hawkes (Ed.).
    • (2009) Advances in Imaging and Electron Physics , pp. 101-121
    • Wall, J.1    Simon, M.2    Hainfeld, J.3
  • 54
    • 42949133898 scopus 로고    scopus 로고
    • Mass mapping of large globin complexes by scanning transmission electron microscopy
    • (Globins and Other Nitric Oxide-Reactive Proteins, Part A)
    • Wall J.S., Simon M.N., Lin B.Y., Vinogradov S.N. Mass mapping of large globin complexes by scanning transmission electron microscopy. Methods Enzymol. 2008, 436:487-501. (Globins and Other Nitric Oxide-Reactive Proteins, Part A).
    • (2008) Methods Enzymol. , vol.436 , pp. 487-501
    • Wall, J.S.1    Simon, M.N.2    Lin, B.Y.3    Vinogradov, S.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.