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Volumn 146, Issue 3, 2004, Pages 441-451

Immobilization of biotinylated DNA on 2-D streptavidin crystals

Author keywords

2 D crystals; Biotinylated DNA; Electron microscopy; Image analysis; RNA Polymerase; Streptavidin

Indexed keywords

DNA; OLIGONUCLEOTIDE; RNA POLYMERASE; STREPTAVIDIN;

EID: 1942521308     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.02.001     Document Type: Article
Times cited : (19)

References (26)
  • 2
    • 0024978067 scopus 로고
    • Promoter-dependent transcription by RNA polymerase II using immobilized enzyme complexes
    • Arias J.A., Dynan W.S. Promoter-dependent transcription by RNA polymerase II using immobilized enzyme complexes. J. Biol. Chem. 264:1989;3223-3229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3223-3229
    • Arias, J.A.1    Dynan, W.S.2
  • 4
    • 0026011793 scopus 로고
    • Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules
    • Darst S.A., Ahlers M., Meller P.H., Kubalek E.W., Blankenburg R., Ribi H.O., Ringsdorf H., Kornberg R.D. Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules. Biophys. J. 59:1991;387-396.
    • (1991) Biophys. J. , vol.59 , pp. 387-396
    • Darst, S.A.1    Ahlers, M.2    Meller, P.H.3    Kubalek, E.W.4    Blankenburg, R.5    Ribi, H.O.6    Ringsdorf, H.7    Kornberg, R.D.8
  • 5
    • 0036427905 scopus 로고    scopus 로고
    • Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles
    • De Carlo S., el Bez C., Alvarez-Rua C., Borge J., Dubochet J. Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles. J. Struct. Biol. 138:2002;216-226.
    • (2002) J. Struct. Biol. , vol.138 , pp. 216-226
    • De Carlo, S.1    El Bez, C.2    Alvarez-Rua, C.3    Borge, J.4    Dubochet, J.5
  • 6
    • 0027418576 scopus 로고
    • The portal protein of bacteriophage SPP1: A DNA pump with 13-fold symmetry
    • Dube P., Tavares P., Lurz R., van Heel M. The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry. EMBO J. 12:1993;1303-1309.
    • (1993) EMBO J. , vol.12 , pp. 1303-1309
    • Dube, P.1    Tavares, P.2    Lurz, R.3    Van Heel, M.4
  • 9
    • 0015041358 scopus 로고
    • A new preparation method for dark-field electron microscopy of biomacromolecules
    • Dubochet J., Ducommun M., Zollinger M., Kellenberger E. A new preparation method for dark-field electron microscopy of biomacromolecules. J. Ultrastruct. Res. 35:1971;147-167.
    • (1971) J. Ultrastruct. Res. , vol.35 , pp. 147-167
    • Dubochet, J.1    Ducommun, M.2    Zollinger, M.3    Kellenberger, E.4
  • 10
    • 84986676687 scopus 로고
    • Phospholipid, nature's own slide and cover slip for cryo-electron microscopy
    • Frederik P.M., Stuart M.C., Bomans P.H., Busing W.M. Phospholipid, nature's own slide and cover slip for cryo-electron microscopy. J. Microsc. 153(Pt 1):1989;81-92.
    • (1989) J. Microsc. , vol.153 , Issue.PT 1 , pp. 81-92
    • Frederik, P.M.1    Stuart, M.C.2    Bomans, P.H.3    Busing, W.M.4
  • 11
    • 0024319092 scopus 로고
    • Magnetic DNA affinity purification of yeast transcription factor tau - A new purification principle for the ultrarapid isolation of near homogeneous factor
    • Gabrielsen O.S., Hornes E., Korsnes L., Ruet A., Oyen T.B. Magnetic DNA affinity purification of yeast transcription factor tau - a new purification principle for the ultrarapid isolation of near homogeneous factor. Nucleic Acids Res. 17:1989;6253-6267.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6253-6267
    • Gabrielsen, O.S.1    Hornes, E.2    Korsnes, L.3    Ruet, A.4    Oyen, T.B.5
  • 12
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 a resolution
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science. 292:2001;1876-1882.
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 13
    • 0033118984 scopus 로고    scopus 로고
    • RNA polymerase II as a control panel for multiple coactivator complexes
    • Hampsey M., Reinberg D. RNA polymerase II as a control panel for multiple coactivator complexes. Curr. Opin. Genet. Dev. 9:1999;132-139.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 132-139
    • Hampsey, M.1    Reinberg, D.2
  • 14
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
    • Heymann J.B., Cheng N., Newcomb W.W., Trus B.L., Brown J.C., Steven A.C. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat. Struct. Biol. 10:2003;334-341.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 15
    • 84985225810 scopus 로고
    • Improved anticontaminator for cryo-electron microscopy with Philips EM400
    • Homo J.C., Booy F.P., Labouesse P., Lepault J., Dubochet J. Improved anticontaminator for cryo-electron microscopy with Philips EM400. J. Microsc. 136:1984;337-340.
    • (1984) J. Microsc. , vol.136 , pp. 337-340
    • Homo, J.C.1    Booy, F.P.2    Labouesse, P.3    Lepault, J.4    Dubochet, J.5
  • 16
    • 84943488666 scopus 로고
    • Ueber Desoxyribonukleinsäure-Molekeln in Protein-Mischfilmen
    • Kleinschmidt A.K., Zahn R.K. Ueber Desoxyribonukleinsäure-Molekeln in Protein-Mischfilmen. Z. Naturforsch. 14B:1959;770-779.
    • (1959) Z. Naturforsch. , vol.14 , pp. 770-779
    • Kleinschmidt, A.K.1    Zahn, R.K.2
  • 17
    • 0025961551 scopus 로고
    • Time-resolved cryo-electron microscopy of vitrified muscular components
    • Lepault J., Erk I., Nicolas G., Ranck J.L. Time-resolved cryo-electron microscopy of vitrified muscular components. J. Microsc. 161(Pt 1):1991;47-57.
    • (1991) J. Microsc. , vol.161 , Issue.PT 1 , pp. 47-57
    • Lepault, J.1    Erk, I.2    Nicolas, G.3    Ranck, J.L.4
  • 19
    • 0032900980 scopus 로고    scopus 로고
    • Intermediates in formation and activity of the RNA polymerase II preinitiation complex: Holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB
    • Ranish J.A., Yudkovsky N., Hahn S. Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB. Genes Dev. 13:1999;49-63.
    • (1999) Genes Dev. , vol.13 , pp. 49-63
    • Ranish, J.A.1    Yudkovsky, N.2    Hahn, S.3
  • 20
    • 0141753120 scopus 로고    scopus 로고
    • The comings and goings of nucleotide excision repair factors on damaged DNA
    • Riedl T., Hanaoka F., Egly J.M. The comings and goings of nucleotide excision repair factors on damaged DNA. EMBO J. 22:2003;5293-5303.
    • (2003) EMBO J. , vol.22 , pp. 5293-5303
    • Riedl, T.1    Hanaoka, F.2    Egly, J.M.3
  • 21
    • 0033386253 scopus 로고    scopus 로고
    • Electron crystallography of bacteriorhodopsin with millisecond time resolution
    • Subramaniam S., Henderson R. Electron crystallography of bacteriorhodopsin with millisecond time resolution. J. Struct. Biol. 128:1999;19-25.
    • (1999) J. Struct. Biol. , vol.128 , pp. 19-25
    • Subramaniam, S.1    Henderson, R.2
  • 22
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. Protein denaturation. Adv. Protein Chem. 23:1968;121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 23
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstruction
    • van Heel M. Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction. Ultramicroscopy. 21:1988;111-124.
    • (1988) Ultramicroscopy , vol.21 , pp. 111-124
    • Van Heel, M.1
  • 24
    • 0029916485 scopus 로고    scopus 로고
    • A new generation of the IMAGIC image processing system
    • van Heel M., Harauz G., Orlova E.V. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116:1996;17-24.
    • (1996) J. Struct. Biol , vol.116 , pp. 17-24
    • Van Heel, M.1    Harauz, G.2    Orlova, E.V.3
  • 25
    • 0008225537 scopus 로고
    • A routine method for protein-free spreading of double- and single-stranded nucleic acid molecules
    • Vollenweider H.J., Sogo J.M., Koller T. A routine method for protein-free spreading of double- and single-stranded nucleic acid molecules. Proc. Natl. Acad. Sci. USA. 72:1975;83-87.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 83-87
    • Vollenweider, H.J.1    Sogo, J.M.2    Koller, T.3
  • 26
    • 0017499528 scopus 로고
    • Use of polylysine for adsorption of nuclei acids and enzymes to electron microscope specimen films
    • Williams R.C. Use of polylysine for adsorption of nuclei acids and enzymes to electron microscope specimen films. Proc. Natl. Acad. Sci. USA. 74:1977;2311-2315.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2311-2315
    • Williams, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.