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Volumn 228, Issue 1, 2007, Pages 25-33

Quantitative STEM mass measurement of biological macromolecules in a 300 kV TEM

Author keywords

Biological macromolecules; Elastic scattering; Hemocyanin; Mass mapping; Scanning transmission electron microscopy; STEM; Tobacco mosaic virus

Indexed keywords

ELASTIC SCATTERING; ELECTRONS; MACROMOLECULES; MAPPING; PROTEINS; SCANNING ELECTRON MICROSCOPY; TOBACCO; VIRUSES;

EID: 34848906043     PISSN: 00222720     EISSN: 13652818     Source Type: Journal    
DOI: 10.1111/j.1365-2818.2007.01819.x     Document Type: Article
Times cited : (22)

References (43)
  • 1
    • 0037168446 scopus 로고    scopus 로고
    • Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance
    • &
    • Antzutkin, O.N., Leapman, R.D., Balbach, J.J. & Tycko, R. (2002) Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. Biochemistry 41, 15436 15450.
    • (2002) Biochemistry , vol.41 , pp. 15436-15450
    • Antzutkin, O.N.1    Leapman, R.D.2    Balbach, J.J.3    Tycko, R.4
  • 2
    • 34848882620 scopus 로고
    • Determination of the total dry mass of human erythrocytes by quantitative electron microscopy
    • &
    • Bahr, G.F. & Zeitler, E. (1962) Determination of the total dry mass of human erythrocytes by quantitative electron microscopy. Lab. Invest. 11, 912 917.
    • (1962) Lab. Invest. , vol.11 , pp. 912-917
    • Bahr, G.F.1    Zeitler, E.2
  • 3
    • 0242353209 scopus 로고    scopus 로고
    • Architecture of Ure2p prion filaments: The N-terminal domains form a central core fiber
    • &
    • Baxa, U., Taylor, K.L., Wall, J.S., Simon, M.N., Cheng, N., Wickner, R.B. & Steven, A.C. (2003) Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber. J. Biol. Chem. 278, 43717 43727.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43717-43727
    • Baxa, U.1    Taylor, K.L.2    Wall, J.S.3    Simon, M.N.4    Cheng, N.5    Wickner, R.B.6    Steven, A.C.7
  • 4
    • 33646857025 scopus 로고    scopus 로고
    • The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis
    • Bergen, M.V., Barghorn, S., Müller, S.A., et al. (2006) The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis. Biochemistry 45, 6446 6457.
    • (2006) Biochemistry , vol.45 , pp. 6446-6457
    • Bergen, M.V.1    Barghorn, S.2    Müller, S.A.3
  • 5
    • 34848853689 scopus 로고
    • Quantitative electron microscopy; Determination of dry mass and thickness in a population of casein particles
    • &
    • Bloom, G. & Zeitler, E. (1959) Quantitative electron microscopy; determination of dry mass and thickness in a population of casein particles. Exp. Cell. Res. 17, 13 21.
    • (1959) Exp. Cell. Res. , vol.17 , pp. 13-21
    • Bloom, G.1    Zeitler, E.2
  • 6
    • 0030564888 scopus 로고    scopus 로고
    • Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: A hinged viral adhesion
    • &
    • Cerritelli, M.E., Wall, J.S., Simon, M.N., Conway, J.F. & Steven, A.C. (1996) Stoichiometry and domainal organization of the long tail-fiber of bacteriophage T4: a hinged viral adhesion. J. Mol. Biol. 260, 767 780.
    • (1996) J. Mol. Biol. , vol.260 , pp. 767-780
    • Cerritelli, M.E.1    Wall, J.S.2    Simon, M.N.3    Conway, J.F.4    Steven, A.C.5
  • 8
    • 84980074290 scopus 로고
    • Relativistic Hartree-Fock X-ray and electron scattering factors
    • &
    • Doyle, P.A. & Turner, P.S. (1968) Relativistic Hartree-Fock X-ray and electron scattering factors. Acta Cryst. A24, 390 397.
    • (1968) Acta Cryst. , vol.24 , pp. 390-397
    • Doyle, P.A.1    Turner, P.S.2
  • 10
    • 0018197443 scopus 로고
    • Molecular weight determination by scanning transmission electron microscopy
    • Engel, A. (1978) Molecular weight determination by scanning transmission electron microscopy. Ultramicroscopy 3, 273 281.
    • (1978) Ultramicroscopy , vol.3 , pp. 273-281
    • Engel, A.1
  • 11
    • 0020463936 scopus 로고
    • Mass determination by electron scattering
    • Engel, A. (1982) Mass determination by electron scattering. Micron 13, 425 436.
    • (1982) Micron , vol.13 , pp. 425-436
    • Engel, A.1
  • 12
    • 0021712016 scopus 로고
    • Imaging of biological structures with the scanning transmission electron microscope
    • &
    • Engel, A. & Reichelt, R. (1984) Imaging of biological structures with the scanning transmission electron microscope. J. Ultra. Res. 88, 105 120.
    • (1984) J. Ultra. Res. , vol.88 , pp. 105-120
    • Engel, A.1    Reichelt, R.2
  • 13
    • 0031170794 scopus 로고    scopus 로고
    • Mass determination by inelastic electron scattering in an energy-filtering transmission electron microscope with slow-scan CCD camera
    • &
    • Feja, B., Dürrenberger, M., Müller, S., Reichelt, R. & Aebi, U. (1997) Mass determination by inelastic electron scattering in an energy-filtering transmission electron microscope with slow-scan CCD camera. J. Struct. Biol. 119, 72 82.
    • (1997) J. Struct. Biol. , vol.119 , pp. 72-82
    • Feja, B.1    Dürrenberger, M.2    Müller, S.3    Reichelt, R.4    Aebi, U.5
  • 14
    • 0032804694 scopus 로고    scopus 로고
    • Molecular mass determination by STEM and EFTEM: A critical comparison
    • &
    • Feja, B. & Aebi, U. (1999) Molecular mass determination by STEM and EFTEM: a critical comparison. Micron 30, 299 307.
    • (1999) Micron , vol.30 , pp. 299-307
    • Feja, B.1    Aebi, U.2
  • 15
    • 0019851405 scopus 로고
    • Comparative mass measurement of biological macromolecules by scanning transmission electron microscopy
    • &
    • Freeman, R. & Leonard, K.R. (1981) Comparative mass measurement of biological macromolecules by scanning transmission electron microscopy. J. Microsc. 122, 275 286.
    • (1981) J. Microsc. , vol.122 , pp. 275-286
    • Freeman, R.1    Leonard, K.R.2
  • 16
    • 0024942004 scopus 로고
    • Scanning transmission electron microscopy study of molluscan hemocyanins in various aggregation states: Comparison with light scattering molecular weights
    • &
    • Hamilton, M.G., Herskovits, T.T., Furcinitti, P.S. & Wall, J.S. (1989) Scanning transmission electron microscopy study of molluscan hemocyanins in various aggregation states: comparison with light scattering molecular weights. J. Ultra. Mol. Struct. Res. 102, 221 228.
    • (1989) J. Ultra. Mol. Struct. Res. , vol.102 , pp. 221-228
    • Hamilton, M.G.1    Herskovits, T.T.2    Furcinitti, P.S.3    Wall, J.S.4
  • 18
    • 10044250206 scopus 로고    scopus 로고
    • The precision of lateral size control in the assembly of corneal collagen fibrils
    • &
    • Holmes, D.F. & Kadler, K.E. (2005) The precision of lateral size control in the assembly of corneal collagen fibrils. J. Mol. Biol. 345, 773 784.
    • (2005) J. Mol. Biol. , vol.345 , pp. 773-784
    • Holmes, D.F.1    Kadler, K.E.2
  • 20
    • 3042775270 scopus 로고    scopus 로고
    • Comparison of electron elastic-scattering cross sections calculated from two commonly used atomic potentials
    • &
    • Jablonski, A., Salvat, F. & Powell, C.J. (2004) Comparison of electron elastic-scattering cross sections calculated from two commonly used atomic potentials. J. Phys. Chem. Ref. Data 33, 409 451.
    • (2004) J. Phys. Chem. Ref. Data , vol.33 , pp. 409-451
    • Jablonski, A.1    Salvat, F.2    Powell, C.J.3
  • 21
    • 2342555690 scopus 로고    scopus 로고
    • Organization of designed nanofibrils assembled from alpha-helical peptides as determined by electron microscopy
    • &
    • Kajava, A.V., Potekhin, S.A., Corradin, G. & Leapman, R.D. (2004) Organization of designed nanofibrils assembled from alpha-helical peptides as determined by electron microscopy. J. Pept. Sci. 10, 291 297.
    • (2004) J. Pept. Sci. , vol.10 , pp. 291-297
    • Kajava, A.V.1    Potekhin, S.A.2    Corradin, G.3    Leapman, R.D.4
  • 22
    • 24144465828 scopus 로고    scopus 로고
    • Characterization of paired helical filaments by scanning transmission electron microscopy
    • &
    • Ksiezak-Reding, H. & Wall, J.S. (2005) Characterization of paired helical filaments by scanning transmission electron microscopy. Microsc. Res. Tech. 67, 126 140.
    • (2005) Microsc. Res. Tech. , vol.67 , pp. 126-140
    • Ksiezak-Reding, H.1    Wall, J.S.2
  • 23
    • 0026580433 scopus 로고
    • Characterization of biological macromolecules by combined mass mapping and electron energy-loss spectroscopy
    • &
    • Leapman, R.D. & Andrews, S.B. (1992) Characterization of biological macromolecules by combined mass mapping and electron energy-loss spectroscopy. J. Microsc. 165, 225 238.
    • (1992) J. Microsc. , vol.165 , pp. 225-238
    • Leapman, R.D.1    Andrews, S.B.2
  • 24
    • 0030812106 scopus 로고    scopus 로고
    • Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy
    • &
    • Leapman, R.D., Gallant, P.E., Reese, T.S. & Andrews, S.B. (1997) Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy. Proc. Natl. Acad. Sci. U.S.A. 94, 7820 7824.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7820-7824
    • Leapman, R.D.1    Gallant, P.E.2    Reese, T.S.3    Andrews, S.B.4
  • 25
    • 0019779251 scopus 로고
    • Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy
    • &
    • Mosesson, M.W., Hainfeld, J., Wall, J. & Haschemeyer, R.H. (1981) Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy. J. Mol. Biol. 153, 695 718.
    • (1981) J. Mol. Biol. , vol.153 , pp. 695-718
    • Mosesson, M.W.1    Hainfeld, J.2    Wall, J.3    Haschemeyer, R.H.4
  • 26
    • 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. (1998) Mass measurement in the scanning transmission electron microscope: a powerful tool for studying membrane proteins. J. Struct. Biol. 121, 219 230.
    • (1998) J. Struct. Biol. , vol.121 , pp. 219-230
    • Müller, S.A.1    Engel, A.2
  • 27
    • 0035239217 scopus 로고    scopus 로고
    • Structure and mass analysis by scanning transmission electron microscopy
    • &
    • Müller, S.A. & Engel, A. (2001) Structure and mass analysis by scanning transmission electron microscopy. Micron 32, 21 31.
    • (2001) Micron , vol.32 , pp. 21-31
    • Müller, S.A.1    Engel, A.2
  • 28
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • &
    • Müller, S.A., Goldie, K.N., Burki, R., Haring, R. & Engel, A. (1992) Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy 46, 317 334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Burki, R.3    Haring, R.4    Engel, A.5
  • 29
    • 84977295671 scopus 로고
    • Dirac-Fock calculations of X-ray scattering factors and contributions to the mean inner potential for electron scattering
    • &
    • Rez, D., Rez, P. & Grant, I. (1994) Dirac-Fock calculations of X-ray scattering factors and contributions to the mean inner potential for electron scattering. Acta Cryst. A50, 481 497.
    • (1994) Acta Cryst. , vol.50 , pp. 481-497
    • Rez, D.1    Rez, P.2    Grant, I.3
  • 30
    • 0041030817 scopus 로고    scopus 로고
    • Scattering cross sections in electron microscopy and analysis
    • Rez, P. (2001) Scattering cross sections in electron microscopy and analysis. Microsc. Microanal. 7, 356 362.
    • (2001) Microsc. Microanal. , vol.7 , pp. 356-362
    • Rez, P.1
  • 31
    • 0037410922 scopus 로고    scopus 로고
    • Comparison of phase contrast transmission electron microscopy with optimized scanning transmission annular dark field imaging for protein imaging
    • Rez, P. (2003) Comparison of phase contrast transmission electron microscopy with optimized scanning transmission annular dark field imaging for protein imaging. Ultramicroscopy 96, 117 124.
    • (2003) Ultramicroscopy , vol.96 , pp. 117-124
    • Rez, P.1
  • 32
    • 11144223234 scopus 로고    scopus 로고
    • Elsepa - Dirac partial-wave calculation of elastic scattering of electrons and positrons by atoms, positive ions and molecules
    • &
    • Salvat, F., Jablonski, A. & Powell, C.J. (2005) Elsepa - Dirac partial-wave calculation of elastic scattering of electrons and positrons by atoms, positive ions and molecules. Comput. Phys. Commun. 165, 157 190.
    • (2005) Comput. Phys. Commun. , vol.165 , pp. 157-190
    • Salvat, F.1    Jablonski, A.2    Powell, C.J.3
  • 33
    • 0030772330 scopus 로고    scopus 로고
    • Scanning transmission electron microscopy mass analysis of fibrillin-containing microfibrils from foetal elastic tissues
    • &
    • Sherratt, M.J., Holmes, D.F., Shuttleworth, C.A. & Kielty, C.M. (1997) Scanning transmission electron microscopy mass analysis of fibrillin-containing microfibrils from foetal elastic tissues. Int. J. Biochem. Cell Biol. 29, 1063 1070.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 1063-1070
    • Sherratt, M.J.1    Holmes, D.F.2    Shuttleworth, C.A.3    Kielty, C.M.4
  • 34
    • 0030886451 scopus 로고    scopus 로고
    • Mass determination, subunit organization and control of oligomerization states of keyhole limpet hemocyanin (KLH)
    • &
    • Söhngen, S.M., Stahlmann, A., Harris, J.R., Müller, S.A., Engel, A. & Markl, J. (1997) Mass determination, subunit organization and control of oligomerization states of keyhole limpet hemocyanin (KLH). Eur. J. Biochem. 248, 602 614.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 602-614
    • Söhngen, S.M.1    Stahlmann, A.2    Harris, J.R.3    Müller, S.A.4    Engel, A.5    Markl, J.6
  • 35
    • 0021014680 scopus 로고
    • Epidermal keratin filaments assembled in vitro have masses-per-unit- length that scale according to average subunit mass: Structural basis for homologous packing of subunits in intermediate filaments
    • &
    • Steven, A.C., Hainfeld, J.F., Trus, B.L., Wall, J.S. & Steinert, P.M. (1983a). Epidermal keratin filaments assembled in vitro have masses-per-unit-length that scale according to average subunit mass: structural basis for homologous packing of subunits in intermediate filaments. J. Cell Biol. 97, 1939 1944.
    • (1983) J. Cell Biol. , vol.97 , pp. 1939-1944
    • Steven, A.C.1    Hainfeld, J.F.2    Trus, B.L.3    Wall, J.S.4    Steinert, P.M.5
  • 36
    • 0021099704 scopus 로고
    • The distribution of mass in heteropolymer intermediate filaments assembled in vitro. Stem analysis of vimentin/desmin and bovine epidermal keratin
    • &
    • Steven, A.C., Hainfeld, J.F., Trus, B.L., Wall, J.S. & Steinert, P.M. (1983b) The distribution of mass in heteropolymer intermediate filaments assembled in vitro. Stem analysis of vimentin/desmin and bovine epidermal keratin. J. Biol. Chem. 258, 8323 8329.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8323-8329
    • Steven, A.C.1    Hainfeld, J.F.2    Trus, B.L.3    Wall, J.S.4    Steinert, P.M.5
  • 37
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • &
    • Thomas, D., Schultz, P., Steven, A.C. & Wall, J.S. (1994) Mass analysis of biological macromolecular complexes by STEM. Biol. Cell 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
  • 38
    • 0038163517 scopus 로고    scopus 로고
    • Imaging individual atoms inside crystals with ADF-STEM
    • &
    • Voyles, P.M, Grazul, J.L. & Muller, D.A. (2003) Imaging individual atoms inside crystals with ADF-STEM. Ultramicroscopy 96, 251 273.
    • (2003) Ultramicroscopy , vol.96 , pp. 251-273
    • Voyles, P.M.1    Grazul, J.L.2    Muller, D.A.3
  • 39
    • 0016027680 scopus 로고
    • The collection of scattered electrons in dark field electron microscopy. II Inelastic scattering
    • &
    • Wall, J., Isaacson, M. & Langmore, J.P. (1974) The collection of scattered electrons in dark field electron microscopy. II Inelastic scattering. Optik, 39, 359 374.
    • (1974) Optik , vol.39 , pp. 359-374
    • Wall, J.1    Isaacson, M.2    Langmore, J.P.3
  • 40
    • 0018581990 scopus 로고
    • Mass measurements with the electron microscope
    • Wall, J.S. (1979) Mass measurements with the electron microscope. Scan. Elect. Microsc. 2, 291 302.
    • (1979) Scan. Elect. Microsc. , vol.2 , pp. 291-302
    • Wall, J.S.1
  • 41
    • 0022526226 scopus 로고
    • Mass mapping with the scanning transmission electron microscope
    • &
    • Wall, J.S. & Hainfeld, J.F. (1986) Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Chem. 15, 335 376.
    • (1986) Annu. Rev. Biophys. Chem. , vol.15 , pp. 335-376
    • Wall, J.S.1    Hainfeld, J.F.2
  • 43
    • 0036421206 scopus 로고    scopus 로고
    • Three-dimensional localization of ultrasmall immuno-gold labels by HAADF-STEM tomography
    • &
    • Ziese, U., Kübel, C., Verkleij, A.J. & Koster, A.J. (2002). Three-dimensional localization of ultrasmall immuno-gold labels by HAADF-STEM tomography. J. Struct. Biol. 138, 58 62.
    • (2002) J. Struct. Biol. , vol.138 , pp. 58-62
    • Ziese, U.1    Kübel, C.2    Verkleij, A.J.3    Koster, A.J.4


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