메뉴 건너뛰기




Volumn 96, Issue 9, 2009, Pages 3822-3831

Structural information, resolution, and noise in high-resolution atomic force microscopy topographs

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ATOMIC FORCE MICROSCOPY; GEOMETRY; IMAGE ANALYSIS; IMAGING; MEASUREMENT ERROR; MOLECULE; NOISE; OPTICAL RESOLUTION; PROTEIN STRUCTURE; TOPOGRAPHY; CHEMISTRY; IMAGE ENHANCEMENT; IMAGE PROCESSING; METHODOLOGY; PROTEIN CONFORMATION;

EID: 67650359926     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.02.011     Document Type: Article
Times cited : (50)

References (41)
  • 2
    • 0042329979 scopus 로고    scopus 로고
    • Robert Feulgen lecture. Microscopic assessment of membrane protein structure and function
    • Engel, A. 2003. Robert Feulgen lecture. Microscopic assessment of membrane protein structure and function. Histochem. Cell Biol. 120:93-102.
    • (2003) Histochem. Cell Biol , vol.120 , pp. 93-102
    • Engel, A.1
  • 3
    • 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
  • 5
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • Fotiadis, D., Y. Liang, S. Filipek, D. A. Saperstein, A. Engel, et al. 2003. Atomic-force microscopy: Rhodopsin dimers in native disc membranes. Nature. 421:127-128.
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5
  • 6
    • 33846014316 scopus 로고    scopus 로고
    • The supramolecular architecture of junctional microdomains in native lens membranes
    • 8:51-55
    • Buzhynskyy, N., R. K. Hite, T. Walz, and S. Scheuring. 2007. The supramolecular architecture of junctional microdomains in native lens membranes. EMBO Rep. 8:51-55.
    • (2007) EMBO Rep
    • Buzhynskyy, N.1    Hite, R.K.2    Walz, T.3    Scheuring, S.4
  • 7
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring, S., and J. N. Sturgis. 2005. Chromatic adaptation of photosynthetic membranes. Science. 309:484-487.
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 8
    • 34447638509 scopus 로고    scopus 로고
    • From high-resolution AFM topographs to atomic models of supramolecular assemblies
    • Scheuring, S., T. Boudier, and J. N. Sturgis. 2007. From high-resolution AFM topographs to atomic models of supramolecular assemblies. J. Struct. Biol. 159:268-276.
    • (2007) J. Struct. Biol , vol.159 , pp. 268-276
    • Scheuring, S.1    Boudier, T.2    Sturgis, J.N.3
  • 9
    • 36049012024 scopus 로고    scopus 로고
    • Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains
    • Scheuring, S., N. Buzhynskyy, S. Jaroslawski, R. P. Gonçalves, R. K. Hite, et al. 2007. Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains. J. Struct. Biol. 160:385-394.
    • (2007) J. Struct. Biol , vol.160 , pp. 385-394
    • Scheuring, S.1    Buzhynskyy, N.2    Jaroslawski, S.3    Gonçalves, R.P.4    Hite, R.K.5
  • 10
    • 0347625831 scopus 로고    scopus 로고
    • Direct observation of Calpha-Halpha...O=C hydrogen bonds in proteins by interresidue h3JCalphaC' scalar couplings
    • Cordier, F., M. Barfield, and S. Grzesiek. 2003. Direct observation of Calpha-Halpha...O=C hydrogen bonds in proteins by interresidue h3JCalphaC' scalar couplings. J. Am. Chem. Soc. 125:15750-15751.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 15750-15751
    • Cordier, F.1    Barfield, M.2    Grzesiek, S.3
  • 11
    • 30044439673 scopus 로고    scopus 로고
    • Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å
    • Lee, J., D. Kozono, J. Remis, Y. Kitagawa, P. Agre, et al. 2005. Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å. Proc. Natl. Acad. Sci. USA. 102:18932-18937.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18932-18937
    • Lee, J.1    Kozono, D.2    Remis, J.3    Kitagawa, Y.4    Agre, P.5
  • 12
    • 0030768310 scopus 로고    scopus 로고
    • Surface of bacteriorhodopsin revealed by high-resolution electron microscopy
    • Kimura, K., D. G. Vassylev, A. Miyazawa, A. Kidera, M. Matsushima, et al. 1997. Surface of bacteriorhodopsin revealed by high-resolution electron microscopy. Nature. 389:206-211.
    • (1997) Nature , vol.389 , pp. 206-211
    • Kimura, K.1    Vassylev, D.G.2    Miyazawa, A.3    Kidera, A.4    Matsushima, M.5
  • 13
    • 0037319733 scopus 로고    scopus 로고
    • Electron microscopy of functional ribosome complexes
    • Frank, J. 2003. Electron microscopy of functional ribosome complexes. Biopolymers. 68:223-233.
    • (2003) Biopolymers , vol.68 , pp. 223-233
    • Frank, J.1
  • 14
    • 0032533456 scopus 로고    scopus 로고
    • The structure of an insect parvovirus (Galleria mellonella densovirus) at 3.7 A resolution
    • Simpson, A., P. Chipman, T. Baker, P. Tijssen, and M. Rossmann. 1998. The structure of an insect parvovirus (Galleria mellonella densovirus) at 3.7 A resolution. Structure. 6:1355-1367.
    • (1998) Structure , vol.6 , pp. 1355-1367
    • Simpson, A.1    Chipman, P.2    Baker, T.3    Tijssen, P.4    Rossmann, M.5
  • 15
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light harvesting complex at 2.5 A resolution
    • Standfuss, J., A. C. Terwisscha van Scheltinga, M. Lamborghini, and W. Kühlbrandt. 2005. Mechanisms of photoprotection and nonphotochemical quenching in pea light harvesting complex at 2.5 A resolution. EMBO J. 24:919-928.
    • (2005) EMBO J , vol.24 , pp. 919-928
    • Standfuss, J.1    Terwisscha van Scheltinga, A.C.2    Lamborghini, M.3    Kühlbrandt, W.4
  • 16
    • 2942631678 scopus 로고    scopus 로고
    • High-resolution imaging of bacteriorhodopsin by atomic force microscopy
    • Fotiadis, D., and A. Engel. 2004. High-resolution imaging of bacteriorhodopsin by atomic force microscopy. Methods Mol. Biol. 242: 291-303.
    • (2004) Methods Mol. Biol , vol.242 , pp. 291-303
    • Fotiadis, D.1    Engel, A.2
  • 17
    • 0019802812 scopus 로고
    • Computer averaging of electron micropgraphs of 40S ribosomal subunits
    • Frank, J., A. Verschoor, and M. Boublik. 1981. Computer averaging of electron micropgraphs of 40S ribosomal subunits. Science. 214: 1353-1355.
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 18
    • 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
  • 19
    • 0023067967 scopus 로고
    • A new resolution criterion based on spectral signal-to-noise ratios
    • Unser, M., B. L. Trus, and A. C. Steven. 1987. A new resolution criterion based on spectral signal-to-noise ratios. Ultramicroscopy. 23: 39-52.
    • (1987) Ultramicroscopy , vol.23 , pp. 39-52
    • Unser, M.1    Trus, B.L.2    Steven, A.C.3
  • 20
    • 0024698772 scopus 로고
    • The spectral signal-to-noise ration resolution criterion: Computational efficiency and statistical precision
    • Unser, M., B. L. Trus, J. Frank, and A. L. Steven. 1989. The spectral signal-to-noise ration resolution criterion: Computational efficiency and statistical precision. Ultramicroscopy. 30:429-434.
    • (1989) Ultramicroscopy , vol.30 , pp. 429-434
    • Unser, M.1    Trus, B.L.2    Frank, J.3    Steven, A.L.4
  • 21
    • 0034698003 scopus 로고    scopus 로고
    • Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence
    • Fotiadis, D., L. Hasler, D. J. Müller, H. Stahlberg, J. Kistler, et al. 2000. Surface tongue-and-groove contours on lens MIP facilitate cell-to-cell adherence. J. Mol. Biol. 300:779-789.
    • (2000) J. Mol. Biol , vol.300 , pp. 779-789
    • Fotiadis, D.1    Hasler, L.2    Müller, D.J.3    Stahlberg, H.4    Kistler, J.5
  • 22
    • 0035979768 scopus 로고    scopus 로고
    • Two-dimensional crystals: A powerful approach to assess structure, function and dynamics of membrane proteins
    • Stahlberg, H., D. Fotiadis, S. Scheuring, H. Remigy, T. Braun, et al. 2001. Two-dimensional crystals: a powerful approach to assess structure, function and dynamics of membrane proteins. FEBS Lett. 504:166-172.
    • (2001) FEBS Lett , vol.504 , pp. 166-172
    • Stahlberg, H.1    Fotiadis, D.2    Scheuring, S.3    Remigy, H.4    Braun, T.5
  • 23
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin, P. N. T., and R. Henderson. 1975. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94:425-440.
    • (1975) J. Mol. Biol , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 24
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson, R., and P. N. T. Unwin. 1975. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 25
    • 0033568641 scopus 로고    scopus 로고
    • High resolution topographs of the Escherichia coli waterchannel aquaporin Z
    • Scheuring, S., P. Ringler, M. Borgina, H. Stahlberg, D. J. Müller, et al. 1999. High resolution topographs of the Escherichia coli waterchannel aquaporin Z. EMBO J. 18:4981-4987.
    • (1999) EMBO J , vol.18 , pp. 4981-4987
    • Scheuring, S.1    Ringler, P.2    Borgina, M.3    Stahlberg, H.4    Müller, D.J.5
  • 26
    • 0033520347 scopus 로고    scopus 로고
    • Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography
    • Ringler, P., M. J. Borgnia, H. Stahlberg, P. C. Maloney, P. Agre, et al. 1999. Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography. J. Mol. Biol. 291:1181-1190.
    • (1999) J. Mol. Biol , vol.291 , pp. 1181-1190
    • Ringler, P.1    Borgnia, M.J.2    Stahlberg, H.3    Maloney, P.C.4    Agre, P.5
  • 27
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckman, et al. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:899-929.
    • (1990) J. Mol. Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckman, E.5
  • 29
    • 0842313156 scopus 로고    scopus 로고
    • Architecture and selectivity in aquaporins: 2.5 a x-ray structure of aquaporin Z
    • Savage, D. F., P. F. Egea, Y. Robles-Colmenares, J. D. O'Connell, and R. M. Stroud. 2003. Architecture and selectivity in aquaporins: 2.5 a x-ray structure of aquaporin Z. PLoS Biol. 1:334-340.
    • (2003) PLoS Biol , vol.1 , pp. 334-340
    • Savage, D.F.1    Egea, P.F.2    Robles-Colmenares, Y.3    O'Connell, J.D.4    Stroud, R.M.5
  • 30
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • Gonen, T., Y. Cheng, P. Sliz, Y. Hiroaki, Y. Fujiyoshi, et al. 2005. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature. 438:633-638.
    • (2005) Nature , vol.438 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5
  • 32
    • 0041841000 scopus 로고    scopus 로고
    • Rasband, W.S. 1997-2005. ImageJ.U.S. National Institutes of Health, Bethesda, Maryland, USA, http://rsb.info.nih.gov/ij/. 33. Müller, D. J., D. Fotiadis, and A. Engel. 1998. Mapping flexible protein domains at subnanometer resolution with the AFM. FEBS Lett. 430:105-111.
    • Rasband, W.S. 1997-2005. ImageJ.U.S. National Institutes of Health, Bethesda, Maryland, USA, http://rsb.info.nih.gov/ij/. 33. Müller, D. J., D. Fotiadis, and A. Engel. 1998. Mapping flexible protein domains at subnanometer resolution with the AFM. FEBS Lett. 430:105-111.
  • 33
    • 0037227427 scopus 로고    scopus 로고
    • AFM characterization of tilt and intrinsic flexibility of Rhodobacter sphaeroides light harvesting complex 2 (LH2)
    • Scheuring, S., J. Seguin, S. Marco, D. Lévy, C. Breyton, et al. 2003. AFM characterization of tilt and intrinsic flexibility of Rhodobacter sphaeroides light harvesting complex 2 (LH2). J. Mol. Biol. 325: 569-580.
    • (2003) J. Mol. Biol , vol.325 , pp. 569-580
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Lévy, D.4    Breyton, C.5
  • 34
  • 35
    • 68949141259 scopus 로고    scopus 로고
    • Malformation of junctional microdomains in type II diabetic cataract lens membranes
    • Submitted
    • Mangenot, S., N. Buzhynskyy, J.-F. Girmens, and S. Scheuring. 2008. Malformation of junctional microdomains in type II diabetic cataract lens membranes. Submitted.
    • (2008)
    • Mangenot, S.1    Buzhynskyy, N.2    Girmens, J.-F.3    Scheuring, S.4
  • 37
    • 9144264281 scopus 로고    scopus 로고
    • Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum
    • Scheuring, S., J.-L. Rigaud, and J. N. Sturgis. 2004. Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum. EMBO J. 23:4127-4133.
    • (2004) EMBO J , vol.23 , pp. 4127-4133
    • Scheuring, S.1    Rigaud, J.-L.2    Sturgis, J.N.3
  • 38
    • 68949140357 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 39
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core-complex in native membranes by AFM
    • Scheuring, S., J. Seguin, S. Marco, D. Levy, B. Robert, et al. 2003. Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core-complex in native membranes by AFM. Proc. Natl. Acad. Sci. USA. 100:1690-1693.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1690-1693
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Levy, D.4    Robert, B.5
  • 40
    • 0035876215 scopus 로고    scopus 로고
    • High resolution topographs of the Rubrivivax gelatinosus light-harvesting complex 2
    • Scheuring, S., F. Reiss-Husson, A. Engel, J.-L. Rigaud, and J.-L. Ranck. 2001. High resolution topographs of the Rubrivivax gelatinosus light-harvesting complex 2. EMBO J. 20:3029-3035.
    • (2001) EMBO J , vol.20 , pp. 3029-3035
    • Scheuring, S.1    Reiss-Husson, F.2    Engel, A.3    Rigaud, J.-L.4    Ranck, J.-L.5
  • 41
    • 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. 1995. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.