메뉴 건너뛰기




Volumn 147, Issue 2, 2004, Pages 136-145

Visualization of α-helical features in a density map constructed using 9 molecular images of the 1.8 MDa icosahedral core of pyruvate dehydrogenase

Author keywords

Electron cryo microscopy; Macromolecular protein complex; Single particle analysis; Three dimensional reconstruction

Indexed keywords

PYRUVATE DEHYDROGENASE;

EID: 2942606544     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.02.007     Document Type: Article
Times cited : (19)

References (26)
  • 1
    • 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
  • 2
    • 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
  • 4
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • DeRosier D., Klug A. Reconstruction of three-dimensional structures from electron micrographs. Nature. 217:1968;130-134
    • (1968) Nature , vol.217 , pp. 130-134
    • Derosier, D.1    Klug, A.2
  • 5
    • 0038670209 scopus 로고    scopus 로고
    • Molecular architecture of the multiprotein splicing factor SF3b
    • Golas M.M., Sander B., Will C.L., Lührmann R., Stark H. Molecular architecture of the multiprotein splicing factor SF3b. Science. 300:2003;980-984
    • (2003) Science , vol.300 , pp. 980-984
    • Golas, M.M.1    Sander, B.2    Will, C.L.3    Lührmann, R.4    Stark, H.5
  • 6
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • Grigorieff N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22. Å in ice J. Mol. Biol. 277:1998;1033-1046
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 7
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • Grigorieff N. Resolution measurement in structures derived from single particles. Acta Crystallogr. D Biol. Crystallogr. 56:2000;1270-1277
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1270-1277
    • Grigorieff, N.1
  • 8
    • 0034903751 scopus 로고    scopus 로고
    • Molray - A web interface between O and the POV-Ray ray tracer
    • Harris M., Jones T.A. Molray - a web interface between O and the POV-Ray ray tracer. Acta Crystallogr. D Biol. Crystallogr. 57:2001;1201-1203
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 10
    • 0033573917 scopus 로고    scopus 로고
    • Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes
    • Izard T., Ævarsson A., Allen M.D., Westphal A.H., Perham R.N., de Kok A., Hol W.G. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc. Natl. Acad. Sci. USA. 96:1999;1240-1245
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1240-1245
    • Izard, T.1    Ævarsson, A.2    Allen, M.D.3    Westphal, A.H.4    Perham, R.N.5    De Kok, A.6    Hol, W.G.7
  • 11
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Jiang W., Li Z., Zhang Z., Baker M.L., Prevelige P.E., Chiu W. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat. Struct. Biol. 10:2003;131-135
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige, P.E.5    Chiu, W.6
  • 12
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 13
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:1999;82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 16
    • 0037119997 scopus 로고    scopus 로고
    • Atomic model of the papillovirus capsid
    • Modis Y., Trus B.L., Harrison S.C. Atomic model of the papillovirus capsid. EMBO J. 21:2002;4754-4762
    • (2002) EMBO J. , vol.21 , pp. 4754-4762
    • Modis, Y.1    Trus, B.L.2    Harrison, S.C.3
  • 17
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69:2000;961-1004
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 18
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333:2003;721-745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 19
    • 0032815040 scopus 로고    scopus 로고
    • Ximdisp - A visualization tool to aid structure determination from electron microscope images
    • Smith J.M. Ximdisp - a visualization tool to aid structure determination from electron microscope images. J. Struct. Biol. 125:1999;223-228
    • (1999) J. Struct. Biol. , vol.125 , pp. 223-228
    • Smith, J.M.1
  • 21
    • 0034802275 scopus 로고    scopus 로고
    • Single-image signal to noise ratio estimation
    • Thong J.T.L., Sim K.S., Phang J.C.H. Single-image signal to noise ratio estimation. Scanning. 23:2001;328-336
    • (2001) Scanning , vol.23 , pp. 328-336
    • Thong, J.T.L.1    Sim, K.S.2    Phang, J.C.H.3
  • 24
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125:1999;185-195
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 26
    • 0035877764 scopus 로고    scopus 로고
    • Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The breathing core and its functional relationship to protein dynamics
    • Zhou Z.H., Liao W., Cheng R.H., Lawson J.E., McCarthy D.B., Reed L.J., Stoops J.K. Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The breathing core and its functional relationship to protein dynamics. J. Biol. Chem. 276:2001;21704-21713
    • (2001) J. Biol. Chem. , vol.276 , pp. 21704-21713
    • Zhou, Z.H.1    Liao, W.2    Cheng, R.H.3    Lawson, J.E.4    McCarthy, D.B.5    Reed, L.J.6    Stoops, J.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.