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Volumn 127, Issue 2, 1999, Pages 169-176

Tetrairidium, a four-atom cluster, is readily visible as a density label in three-dimensional cryo-EM maps of proteins at 10-25 Å resolution

Author keywords

Cryo electron microscopy; Hepatitis B virus; Metal cluster; Molecular marker; Three dimensional image reconstruction

Indexed keywords

CAPSID PROTEIN; IRIDIUM COMPLEX; VIRUS PROTEIN;

EID: 0032751908     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1999.4120     Document Type: Article
Times cited : (51)

References (31)
  • 2
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T. S., Cheng R. H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116:1996;120-130.
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 3
    • 0000397748 scopus 로고
    • Synthesis of water-soluble undecagold cluster compounds of potential importance in electron microscopic and other studies of biological systems
    • Bartlett P. A., Bauer B., Singer S. J. Synthesis of water-soluble undecagold cluster compounds of potential importance in electron microscopic and other studies of biological systems. J. Am. Chem. Soc. 100:1978;5085-5092.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 5085-5092
    • Bartlett, P.A.1    Bauer, B.2    Singer, S.J.3
  • 4
    • 0028869404 scopus 로고
    • Colloidal gold post-embedding immunocytochemistry
    • Bendayan M. Colloidal gold post-embedding immunocytochemistry. Prog. Histochem. Cytochem. 9:1995;1-25.
    • (1995) Prog. Histochem. Cytochem. , vol.9 , pp. 1-25
    • Bendayan, M.1
  • 5
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S. A., Crowther R. A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature. 386:1997;88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 7
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J. F., Cheng N., Zlotnick A., Wingfield P. T., Stahl S. J., Steven A. C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature. 386:1997;91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 8
    • 0032428377 scopus 로고    scopus 로고
    • Localization of the N-terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy
    • Conway J. F., Cheng N., Zlotnick A., Stahl S. J., Wingfield P. T., Steven A. C. Localization of the N-terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy. Proc. Natl. Acad. Sci. USA. 95:1998;14622-14627.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14622-14627
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Stahl, S.J.4    Wingfield, P.T.5    Steven, A.C.6
  • 9
    • 0027959456 scopus 로고
    • Electron microscopy of cytochrome c oxidase crystals: Labeling of subunit III with a monomaleimide undecagold cluster compound
    • Crum J., Gruys K. J., Frey T. G. Electron microscopy of cytochrome c oxidase crystals: Labeling of subunit III with a monomaleimide undecagold cluster compound. Biochemistry. 33:1994;13719-13726.
    • (1994) Biochemistry , vol.33 , pp. 13719-13726
    • Crum, J.1    Gruys, K.J.2    Frey, T.G.3
  • 10
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles: "the uncommon line,"
    • Fuller S. D., Butcher S. J., Cheng R. H., Baker T. S. Three-dimensional reconstruction of icosahedral particles: "The uncommon line," J. Struct. Biol. 116:1996;48-55.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 13
    • 0031026231 scopus 로고    scopus 로고
    • Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro
    • Gregori L., Hainfeld J. F., Simon M. N., Goldgaber D. Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro. J. Biol. Chem. 272:1997;58-62.
    • (1997) J. Biol. Chem. , vol.272 , pp. 58-62
    • Gregori, L.1    Hainfeld, J.F.2    Simon, M.N.3    Goldgaber, D.4
  • 15
    • 0026523922 scopus 로고
    • Site specific cluster labels
    • Hainfeld J. F. Site specific cluster labels. Ultramicroscopy. 46:1992;135-144.
    • (1992) Ultramicroscopy , vol.46 , pp. 135-144
    • Hainfeld, J.F.1
  • 16
    • 0026536069 scopus 로고
    • A 1.4-nm gold cluster covalently attached to antibodies improves immunolabeling
    • Hainfeld J. F., Furuya F. R. A 1.4-nm gold cluster covalently attached to antibodies improves immunolabeling. J. Histochem. Cytochem. 40:1992;177-184.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 177-184
    • Hainfeld, J.F.1    Furuya, F.R.2
  • 17
    • 0030311262 scopus 로고    scopus 로고
    • Labeling with Nanogold and undecagold: Techniques and results
    • Malecki, M., and Roomans, G. M. (Eds.), Scanning Microscopy Int'l, Chicago
    • Hainfeld, J. F.1996Labeling with Nanogold and undecagold: Techniques and results, Scanning Microsc. Suppl. (Proc. 14th Pfefferkorn Conf.)10, 309-322. [Malecki, M., and Roomans, G. M. (Eds.), Scanning Microscopy Int'l, Chicago].
    • (1996) Scanning Microsc. Suppl. (Proc. 14th Pfefferkorn Conf.) , vol.10 , pp. 309-322
    • Hainfeld, J.F.1
  • 18
    • 0008340711 scopus 로고    scopus 로고
    • Nanogold technology: New frontiers in gold labeling
    • Hainfeld J. F., Powell R. D. Nanogold technology: New frontiers in gold labeling. Cell Vision. 4:1997;408-432.
    • (1997) Cell Vision , vol.4 , pp. 408-432
    • Hainfeld, J.F.1    Powell, R.D.2
  • 19
    • 84861177545 scopus 로고
    • Synthesis of water soluble tetrairidium clusters suitable for heavy atom labelling of proteins
    • Jahn W. Synthesis of water soluble tetrairidium clusters suitable for heavy atom labelling of proteins. Z. Naturforsch. B. 44:1989;79-82.
    • (1989) Z. Naturforsch. B , vol.44 , pp. 79-82
    • Jahn, W.1
  • 20
    • 0018568649 scopus 로고
    • Visualization of polymercuri-methane-labeled fd bacteriophage in the scanning transmission electron microscope
    • Lipka J. J., Lippard S. J., Wall J. S. Visualization of polymercuri-methane-labeled fd bacteriophage in the scanning transmission electron microscope. Science. 206:1979;1419-1421.
    • (1979) Science , vol.206 , pp. 1419-1421
    • Lipka, J.J.1    Lippard, S.J.2    Wall, J.S.3
  • 21
    • 0025052483 scopus 로고
    • Molecular structure of F-actin and location of surface binding sites
    • Milligan R. A., Whittaker M., Safer D. Molecular structure of F-actin and location of surface binding sites. Nature. 348:1990;217-221.
    • (1990) Nature , vol.348 , pp. 217-221
    • Milligan, R.A.1    Whittaker, M.2    Safer, D.3
  • 23
    • 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. (Oxford). 127:1982;127-138.
    • (1982) J. Microsc. (Oxford) , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 25
    • 0030931283 scopus 로고    scopus 로고
    • Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution
    • Trus B. L., Roden R. B., Greenstone H. L., Vrhel M., Schiller J. T., Booy F. P. Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution. Nat. Struct. Biol. 4:1997;413-420.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 413-420
    • Trus, B.L.1    Roden, R.B.2    Greenstone, H.L.3    Vrhel, M.4    Schiller, J.T.5    Booy, F.P.6
  • 26
    • 0023090371 scopus 로고
    • Similarity between images
    • Van Heel M. Similarity between images. Ultramicroscopy. 21:1987;95-100.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 27
    • 0024793118 scopus 로고
    • Novel procedures for derivatization of ribosomes for crystallographic studies
    • Weinstein S., Jahn W., Hansen H., Wittmann H. G., Yonath A. Novel procedures for derivatization of ribosomes for crystallographic studies. J. Biol. Chem. 264:1989;19138-19142.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19138-19142
    • Weinstein, S.1    Jahn, W.2    Hansen, H.3    Wittmann, H.G.4    Yonath, A.5
  • 28
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel T., Baumeister W. Conformational constraints in protein degradation by the 20S proteasome. Nat. Struct. Biol. 2:1995;199-204.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 29
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield P. T., Stahl S. J., Williams R. W., Steven A. C. Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry. 34:1995;4919-4932.
    • (1995) Biochemistry , vol.34 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 30
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick A., Cheng N., Conway J. F., Booy F. P., Steven A. C., Stahl S. J., Wingfield P. T. Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry. 35:1996;7412-7421.
    • (1996) Biochemistry , vol.35 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3    Booy, F.P.4    Steven, A.C.5    Stahl, S.J.6    Wingfield, P.T.7
  • 31
    • 0030930426 scopus 로고    scopus 로고
    • Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: Implications for morphogenesis and organization of encapsidated RNA
    • Zlotnick A., Cheng N., Stahl S. J., Conway J. F., Steven A. C., Wingfield P. T. Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: Implications for morphogenesis and organization of encapsidated RNA. Proc. Natl. Acad. Sci. USA. 94:1997;9556-9561.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9556-9561
    • Zlotnick, A.1    Cheng, N.2    Stahl, S.J.3    Conway, J.F.4    Steven, A.C.5    Wingfield, P.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.