메뉴 건너뛰기




Volumn 76, Issue 2, 1999, Pages 1101-1111

Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ATOMIC FORCE MICROSCOPY; ELECTRICITY; IMAGE PROCESSING; IMAGING; MOLECULAR DYNAMICS; PROTEIN LOCALIZATION; SURFACE CHARGE;

EID: 0039114981     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77275-9     Document Type: Article
Times cited : (297)

References (61)
  • 1
    • 0023053025 scopus 로고
    • Three-dimensional structure of the regular surface layer (HPI-layer) of Deinococcus radiodurans
    • Baumeister, W., M. Barth, R. Hegerl, R. Guckenberger, M. Hahn, and W. O. Saxton. 1986. Three-dimensional structure of the regular surface layer (HPI-layer) of Deinococcus radiodurans. J. Mol. Biol. 187: 241-253.
    • (1986) J. Mol. Biol. , vol.187 , pp. 241-253
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 3
    • 0023953848 scopus 로고
    • Bacterial surface proteins: Some structural, functional and evolutionary aspects
    • Baumeister, W., I. Wildhaber, and H. Engelhardt. 1988. Bacterial surface proteins: some structural, functional and evolutionary aspects. Biophys. Chem. 29:39-49.
    • (1988) Biophys. Chem. , vol.29 , pp. 39-49
    • Baumeister, W.1    Wildhaber, I.2    Engelhardt, H.3
  • 5
    • 0026499357 scopus 로고
    • Has negative stain still a place in biomacromolecular electron microscopy?
    • Bremer, A., C. Henn, A. Engel, W. Baumeister, and U. Aebi. 1992. Has negative stain still a place in biomacromolecular electron microscopy? Ultramicroscopy 46:85-111.
    • (1992) Ultramicroscopy , vol.46 , pp. 85-111
    • Bremer, A.1    Henn, C.2    Engel, A.3    Baumeister, W.4    Aebi, U.5
  • 6
    • 0026038548 scopus 로고
    • Electrostatic interaction in atomic force microscopy
    • Butt, H.-J. 1991a. Electrostatic interaction in atomic force microscopy. Biophys. J. 60:777-785.
    • (1991) Biophys. J. , vol.60 , pp. 777-785
    • Butt, H.-J.1
  • 7
    • 0026317248 scopus 로고
    • Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope
    • Butt, H.-J. 1991b. Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope. Biophys. J. 60:1438-1444.
    • (1991) Biophys. J. , vol.60 , pp. 1438-1444
    • Butt, H.-J.1
  • 8
    • 0002549590 scopus 로고
    • Electrostatic interaction in scanning probe microscopy when imaging in electrolyte solutions
    • Butt, H.-J. 1992a. Electrostatic interaction in scanning probe microscopy when imaging in electrolyte solutions. Nanotechnol. 3:60-68.
    • (1992) Nanotechnol. , vol.3 , pp. 60-68
    • Butt, H.-J.1
  • 9
    • 0026657705 scopus 로고
    • Measuring local surface charge densities in electrolyte solutions with a scanning force microscope
    • Butt, H.-J. 1992b. Measuring local surface charge densities in electrolyte solutions with a scanning force microscope. Biophys. J. 63:578-582.
    • (1992) Biophys. J. , vol.63 , pp. 578-582
    • Butt, H.-J.1
  • 10
    • 11744267490 scopus 로고
    • Measuring surface forces in aqueous solution with the atomic force microscope
    • Butt, H.-J., M. Jaschke, and W. Ducker. 1995. Measuring surface forces in aqueous solution with the atomic force microscope. Bioelect. Bioenerg. 38:191-201.
    • (1995) Bioelect. Bioenerg. , vol.38 , pp. 191-201
    • Butt, H.-J.1    Jaschke, M.2    Ducker, W.3
  • 11
    • 0000711515 scopus 로고
    • Imaging purple membranes dry and in water with the atomic force microscope
    • Butt, H.-J., C. B. Prater, and P. K. Hansma. 1991. Imaging purple membranes dry and in water with the atomic force microscope. J. Vac. Sci. Technol. B 9:1193-1197.
    • (1991) J. Vac. Sci. Technol. B , vol.9 , pp. 1193-1197
    • Butt, H.-J.1    Prater, C.B.2    Hansma, P.K.3
  • 12
    • 0001213386 scopus 로고
    • Probing oscillatory hydration potentials using thermal-mechanical noise in an atomic force microscope
    • Cleveland, J. P., T. E. Schäffer, and P. K. Hansma. 1995. Probing oscillatory hydration potentials using thermal-mechanical noise in an atomic force microscope. Phys. Rev. B 52: R8692-R8695.
    • (1995) Phys. Rev. B , vol.52
    • Cleveland, J.P.1    Schäffer, T.E.2    Hansma, P.K.3
  • 14
    • 0032127926 scopus 로고    scopus 로고
    • Direct visualization of surface charge in aqueous solution
    • Czajkowsky, D. M., M. J. Allen, V. Elings, and Z. Shao. 1998b. Direct visualization of surface charge in aqueous solution. Ultramicroscopy. 74:1-5.
    • (1998) Ultramicroscopy , vol.74 , pp. 1-5
    • Czajkowsky, D.M.1    Allen, M.J.2    Elings, V.3    Shao, Z.4
  • 15
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky, D. M., S. Sheng, and Z. Shao. 1998a. Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276:325-330.
    • (1998) J. Mol. Biol. , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 17
    • 0028949325 scopus 로고
    • Binding strength between cell adhesion proteoglycans measured by atomic force microscopy
    • Dammer, U., O. Popescu, P. Wagner, D. Anselmetti, H. J. Güntherodt, and G. N. Misevic. 1995. Binding strength between cell adhesion proteoglycans measured by atomic force microscopy. Science. 267:1173-1175.
    • (1995) Science , vol.267 , pp. 1173-1175
    • Dammer, U.1    Popescu, O.2    Wagner, P.3    Anselmetti, D.4    Güntherodt, H.J.5    Misevic, G.N.6
  • 19
    • 12044257837 scopus 로고
    • Direct measurements of colloidal forces using an atomic force microscope
    • Ducker, W. A., T. J. Senden, and R. M. Pashley. 1991. Direct measurements of colloidal forces using an atomic force microscope. Nature. 353:239-241.
    • (1991) Nature , vol.353 , pp. 239-241
    • Ducker, W.A.1    Senden, T.J.2    Pashley, R.M.3
  • 20
    • 0025855016 scopus 로고
    • Biological applications of scanning probe microscopy
    • Engel, A. 1991. Biological applications of scanning probe microscopy. Annu. Rev. Biophys. Chem. 20:79-108.
    • (1991) Annu. Rev. Biophys. Chem. , vol.20 , pp. 79-108
    • Engel, A.1
  • 21
    • 0030951962 scopus 로고    scopus 로고
    • High-resolution imaging of native biological sample surfaces using scanning probe microscopy
    • Engel, A., C.-A. Schoenenberger, and D. J. Müller. 1997. High-resolution imaging of native biological sample surfaces using scanning probe microscopy. Curr. Opin. Struct. Biol. 7:279-284.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 279-284
    • Engel, A.1    Schoenenberger, C.-A.2    Müller, D.J.3
  • 22
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin, E.-L., V. T. Moy, and H. E. Gaub. 1994. Adhesion forces between individual ligand-receptor pairs. Science. 264:415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.-L.1    Moy, V.T.2    Gaub, H.E.3
  • 24
    • 0031848845 scopus 로고    scopus 로고
    • Hydration force in the atomic force microscope: A computational study
    • Ho, R., J. Y. Yuan, and Z. Shao. 1998. Hydration force in the atomic force microscope: a computational study. Biophys. J. 75:1076-1083.
    • (1998) Biophys. J. , vol.75 , pp. 1076-1083
    • Ho, R.1    Yuan, J.Y.2    Shao, Z.3
  • 25
    • 0027881814 scopus 로고
    • Direct in situ structural analysis of recombinant outer membrane proteins expressed in an OmpA-deficient mutant Escherichia coli strain
    • Hoenger, A., R. Ghosh, C.-A. Schoenenberger, U. Aebi, and A. Engel. 1993. Direct in situ structural analysis of recombinant outer membrane proteins expressed in an OmpA-deficient mutant Escherichia coli strain. J. Struct. Biol. 111:212-221.
    • (1993) J. Struct. Biol. , vol.111 , pp. 212-221
    • Hoenger, A.1    Ghosh, R.2    Schoenenberger, C.-A.3    Aebi, U.4    Engel, A.5
  • 26
    • 0027163746 scopus 로고
    • Structure of the extracellular surface of the gap junction by atomic force microscopy
    • Hoh, J. H., G. E. Sosinsky, J.-P. Revel, and P. K. Hansma. 1993. Structure of the extracellular surface of the gap junction by atomic force microscopy. Biophys. J. 65:149-163.
    • (1993) Biophys. J. , vol.65 , pp. 149-163
    • Hoh, J.H.1    Sosinsky, G.E.2    Revel, J.-P.3    Hansma, P.K.4
  • 29
    • 0028087275 scopus 로고
    • Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment
    • Karrasch, S., R. Hegerl, J. Hoh, W. Baumeister, and A. Engel. 1994. Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc. Natl. Acad. Sci. USA. 91:836-838.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 836-838
    • Karrasch, S.1    Hegerl, R.2    Hoh, J.3    Baumeister, W.4    Engel, A.5
  • 30
    • 0026206391 scopus 로고
    • Reconstruction of STM and AFM images distorted by finite-size tips
    • Keller, D. 1991. Reconstruction of STM and AFM images distorted by finite-size tips. Surf. Sci. 253:353-364.
    • (1991) Surf. Sci. , vol.253 , pp. 353-364
    • Keller, D.1
  • 31
    • 0028007197 scopus 로고
    • Direct measurements of the forces between complementary strands of DNA
    • Lee, G. U., L. A. Chrisey, and R. J. Colton. 1994a. Direct measurements of the forces between complementary strands of DNA. Science. 266: 771-773.
    • (1994) Science , vol.266 , pp. 771-773
    • Lee, G.U.1    Chrisey, L.A.2    Colton, R.J.3
  • 32
    • 0028381539 scopus 로고
    • Sensing discrete streptavidin-biotin interactions with atomic force microscopy
    • Lee, G. U., D. A. Kidwell, and R. J. Colton. 1994b. Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmuir. 10:354-357.
    • (1994) Langmuir , vol.10 , pp. 354-357
    • Lee, G.U.1    Kidwell, D.A.2    Colton, R.J.3
  • 33
    • 0030029859 scopus 로고    scopus 로고
    • High resolution surface structure of E. coli GroES oligomer by atomic force microscopy
    • Mou, J., D. M. Czajkowsky, S. Sheng, R. Ho, and Z. Shao. 1996. High resolution surface structure of E. coli GroES oligomer by atomic force microscopy. FEBS Lett. 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
  • 34
    • 0029069245 scopus 로고
    • Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids
    • Mou, J. X., J. Yang, and Z. F. Shao. 1995. Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids. J. Mol. Biol. 248:507-512.
    • (1995) J. Mol. Biol. , vol.248 , pp. 507-512
    • Mou, J.X.1    Yang, J.2    Shao, Z.F.3
  • 35
    • 0028766095 scopus 로고
    • Adhesive forces between ligand and receptor measured by AFM
    • Moy, V. T., E.-L. Florin, and H. E. Gaub. 1994. Adhesive forces between ligand and receptor measured by AFM. Coll. Surf. A93:343-348.
    • (1994) Coll. Surf. , vol.A93 , pp. 343-348
    • Moy, V.T.1    Florin, E.-L.2    Gaub, H.E.3
  • 36
    • 4244186285 scopus 로고    scopus 로고
    • pH and voltage induced structural changes of porin OmpF explain channel closure
    • in press
    • Müller, D. J., and A. Engel. 1998. pH and voltage induced structural changes of porin OmpF explain channel closure. J. Mol. Biol. (in press)
    • (1998) J. Mol. Biol.
    • Müller, D.J.1    Engel, A.2
  • 37
    • 0041841000 scopus 로고    scopus 로고
    • Mapping flexible protein domains at subnanometer resolution with the AFM
    • Müller, D. J., D. Fotiadis, and A. Engel. 1998. Mapping flexible protein domains at subnanometer resolution with the AFM. FEBS Lett. 430: 105-111.
    • (1998) FEBS Lett. , vol.430 , pp. 105-111
    • Müller, D.J.1    Fotiadis, D.2    Engel, A.3
  • 38
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • In press
    • Müller, D. J., H.-J. Sass, S. Müller, G. Büldt, and A. Engel. 1999. Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J. Mol Biol. In press.
    • (1999) J. Mol Biol.
    • Müller, D.J.1    Sass, H.-J.2    Müller, S.3    Büldt, G.4    Engel, A.5
  • 39
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • Müller, D. J., and A. Engel. 1997. The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73:1633-1644.
    • (1997) Biophys. J. , vol.73 , pp. 1633-1644
    • Müller, D.J.1    Engel, A.2
  • 40
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • Müller, D. J., M. Amrein, and A. Engel. 1997a. Adsorption of biological molecules to a solid support for scanning probe microscopy. J. Struct. Biol. 119:172-188.
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Müller, D.J.1    Amrein, M.2    Engel, A.3
  • 41
    • 0342890045 scopus 로고    scopus 로고
    • Preparation techniques for the observation of native biological systems with the atomic force microscope
    • Müller, D. J., A. Engel, and M. Amrein. 1997b. Preparation techniques for the observation of native biological systems with the atomic force microscope. Biosens. Bioelect. 12:867-877.
    • (1997) Biosens. Bioelect. , vol.12 , pp. 867-877
    • Müller, D.J.1    Engel, A.2    Amrein, M.3
  • 42
    • 0343811707 scopus 로고    scopus 로고
    • The bacteriophage ø29 head-tail connector imaged at high resolution with atomic force microscopy in buffer solution
    • Müller, D. J., A. Engel, J. Carrascosa, and M. Veléz. 1997c. The bacteriophage ø29 head-tail connector imaged at high resolution with atomic force microscopy in buffer solution. EMBO J. 16:101-107.
    • (1997) EMBO J. , vol.16 , pp. 101-107
    • Müller, D.J.1    Engel, A.2    Carrascosa, J.3    Veléz, M.4
  • 43
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes of native membrane proteins monitored at subnanometer resolution with the atomic force microscope
    • Müller, D. J., C.-A. Schoenenberger, F. Schabert, and A. Engel. 1997d. Structural changes of native membrane proteins monitored at subnanometer resolution with the atomic force microscope. J. Struct. Biol. 119: 149-157.
    • (1997) J. Struct. Biol. , vol.119 , pp. 149-157
    • Müller, D.J.1    Schoenenberger, C.-A.2    Schabert, F.3    Engel, A.4
  • 45
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy
    • Müller, D. J., W. Baumeister, and A. Engel. 1996b. Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans imaged by atomic force microscopy. J. Bacteriol. 178: 3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, D.J.1    Baumeister, W.2    Engel, A.3
  • 46
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • Müller, D. J., G. Büldt, and A. Engel. 1995a. Force-induced conformational change of bacteriorhodopsin. J. Mol. Biol. 249:239-243.
    • (1995) J. Mol. Biol. , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 47
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at subnanometer resolution by atomic force microscopy
    • Müller, D. J., F. A. Schabert, G. Büldt, and A. Engel. 1995b. Imaging purple membranes in aqueous solutions at subnanometer resolution by atomic force microscopy. Biophys. J. 68:1681-1686.
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Müller, D.J.1    Schabert, F.A.2    Büldt, G.3    Engel, A.4
  • 48
    • 0032516205 scopus 로고    scopus 로고
    • The molecular elasticity of the extracellular matrix protein tenascin
    • Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:181-185.
    • (1998) Nature , vol.393 , pp. 181-185
    • Oberhauser, A.F.1    Marszalek, P.E.2    Erickson, H.P.3    Fernandez, J.M.4
  • 49
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fraction into red and purple membrane
    • Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fraction into red and purple membrane. Methods Enzymol. 31:667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 50
    • 0015396878 scopus 로고
    • On the electrostatic interaction across a salt solution between two bodies bearing unequal charges
    • Parsegian, V. A., and D. Gingell. 1972. On the electrostatic interaction across a salt solution between two bodies bearing unequal charges. Biophys. J. 12:1192-1204.
    • (1972) Biophys. J. , vol.12 , pp. 1192-1204
    • Parsegian, V.A.1    Gingell, D.2
  • 52
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 53
    • 4243277794 scopus 로고    scopus 로고
    • Mapping local electrostatic forces with the atomic force microscope
    • Rotsch, C., and M. Radmacher. 1997. Mapping local electrostatic forces with the atomic force microscope. Langmuir. 13:2825-2832.
    • (1997) Langmuir , vol.13 , pp. 2825-2832
    • Rotsch, C.1    Radmacher, M.2
  • 54
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton, W. O., and W. Baumeister. 1982. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127: 127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 55
    • 0018650401 scopus 로고
    • Digital image processing: The semper system
    • Saxton, W. O., T. J. Pitt, and M. Horner. 1979. Digital image processing: the semper system. Ultramicroscopy. 4:343-354.
    • (1979) Ultramicroscopy , vol.4 , pp. 343-354
    • Saxton, W.O.1    Pitt, T.J.2    Horner, M.3
  • 56
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert, F. A., C. Henn, and A. Engel. 1995. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science. 268:92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 57
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
    • Schabert, F. A., and A. Engel. 1994. Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy. Biophys. J. 67:2394-2403.
    • (1994) Biophys. J. , vol.67 , pp. 2394-2403
    • Schabert, F.A.1    Engel, A.2
  • 59
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: What is achieved and what is needed
    • Shao, Z., J. Mou, D. M. Czajkowsky, J. Yang, and J.-Y. Yuan. 1996. Biological atomic force microscopy: what is achieved and what is needed. Adv. Phys. 45:1-86.
    • (1996) Adv. Phys. , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czajkowsky, D.M.3    Yang, J.4    Yuan, J.-Y.5
  • 61
    • 84918249181 scopus 로고
    • The transition metal dichalcogenides: Discussion and interpretation of the observed optical, electrical and structural properties
    • Wilson, J. A., and A. D. Yoffe. 1969. The transition metal dichalcogenides: discussion and interpretation of the observed optical, electrical and structural properties. Advanc. Phys. 18:193-335.
    • (1969) Advanc. Phys. , vol.18 , pp. 193-335
    • Wilson, J.A.1    Yoffe, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.