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Volumn 121, Issue 1, 1997, Pages 1-4

Crystallization of eukaryotic E3, lipoamide dehydrogenase, from yeast, for exhibiting X-ray diffraction beyond 2.5 Å resolution, and preliminary structure analysis

Author keywords

Crystallization; Lipoamide dehydrogenase; X ray study

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE;

EID: 0031032913     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021550     Document Type: Article
Times cited : (4)

References (20)
  • 1
    • 2642644904 scopus 로고
    • Multienzyme complexes
    • Reed, L.J. (1974) Multienzyme complexes. Acc. Chem. Res. 7, 701-729
    • (1974) Acc. Chem. Res. , vol.7 , pp. 701-729
    • Reed, L.J.1
  • 2
    • 0025370816 scopus 로고
    • Structure-function relationships in dehydrolipoamide acyltransferases
    • Reed, L.J. (1990) Structure-function relationships in dehydrolipoamide acyltransferases. J. Biol. Chem. 265, 8971-8974
    • (1990) J. Biol. Chem. , vol.265 , pp. 8971-8974
    • Reed, L.J.1
  • 3
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenese multienzyme complexes: A paradigm in the design of a multifunctional protein
    • Perpham, R.N. (1991) Domains, motifs, and linkers in 2-oxo acid dehydrogenese multienzyme complexes: A paradigm in the design of a multifunctional protein. Biochemistry 30, 8501-8512
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perpham, R.N.1
  • 4
    • 0024578239 scopus 로고
    • The 2-oxo acid dehydrogenase complexes: Recent advances
    • Yeaman, S.J. (1989) The 2-oxo acid dehydrogenase complexes: recent advances. Biochem. J. 257, 625-632
    • (1989) Biochem. J. , vol.257 , pp. 625-632
    • Yeaman, S.J.1
  • 5
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel, M.S. (1990) Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4, 3224-3233
    • (1990) FASEB J. , vol.4 , pp. 3224-3233
    • Patel, M.S.1
  • 6
    • 0025816177 scopus 로고
    • Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution
    • Mattevi, A., Schierbeek, A.J., and Hol, W.G.J. (1991) Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution, J. Mol. Biol. 220, 975-994
    • (1991) J. Mol. Biol. , vol.220 , pp. 975-994
    • Mattevi, A.1    Schierbeek, A.J.2    Hol, W.G.J.3
  • 7
    • 0027173717 scopus 로고
    • Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescence at 2.8 Å resolution
    • Mattevi, A., Obmolova, G., Kalk, K.H., van Berkel, W.J.H., and Hol, W.G.J. (1993) Three-dimensional structure of lipoamide dehydrogenase from Pseudomonas fluorescence at 2.8 Å resolution. J. Mol. Biol. 230, 1200-1215
    • (1993) J. Mol. Biol. , vol.230 , pp. 1200-1215
    • Mattevi, A.1    Obmolova, G.2    Kalk, K.H.3    Van Berkel, W.J.H.4    Hol, W.G.J.5
  • 8
    • 0023971592 scopus 로고
    • X-ray study of Baker's yeast lipoamide dehydrogenase at 4.5 Å resolution by molecular replacement method
    • Takenaka, A., Kizawa, K., Hata, T., Sato, S., Misaka, E., Tamura, C., and Sasada, Y. (1988) X-ray study of Baker's yeast lipoamide dehydrogenase at 4.5 Å resolution by molecular replacement method. J. Biochem. 103, 463-469
    • (1988) J. Biochem. , vol.103 , pp. 463-469
    • Takenaka, A.1    Kizawa, K.2    Hata, T.3    Sato, S.4    Misaka, E.5    Tamura, C.6    Sasada, Y.7
  • 9
    • 0014241533 scopus 로고
    • Purification and properties of lipoamide dehydrogenase from yeast, Candida krusei
    • Kawahara, Y., Misaka, E., and Nakanishi, K. (1968) Purification and properties of lipoamide dehydrogenase from yeast, Candida krusei. J. Biochem. 63, 77-82
    • (1968) J. Biochem. , vol.63 , pp. 77-82
    • Kawahara, Y.1    Misaka, E.2    Nakanishi, K.3
  • 10
    • 0001752523 scopus 로고
    • Studies on the nature and reactions of protein-bound lipoic acid
    • Reed, L.J., Koike, M., Levitch, M.E., and Leach, F.R. (1958) Studies on the nature and reactions of protein-bound lipoic acid. J. Biol. Chem. 232, 143-158
    • (1958) J. Biol. Chem. , vol.232 , pp. 143-158
    • Reed, L.J.1    Koike, M.2    Levitch, M.E.3    Leach, F.R.4
  • 11
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for moderm protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation
    • Sakabe, N. (1991) X-ray diffraction data collection system for moderm protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. Methods A303, 448-463
    • (1991) Nucl. Instrum. Methods , vol.A303 , pp. 448-463
    • Sakabe, N.1
  • 12
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography
    • Higashi, T. (1989) The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J. Appl. Cryst. 22, 9-18
    • (1989) J. Appl. Cryst. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 13
    • 0003790828 scopus 로고
    • A suite of programs for protein crystallography
    • Daresbury Laboratory, Warrington UK
    • A suite of programs for protein crystallography (SERC Collaborative Computing Project No. 4, Daresbury Laboratory, Warrington UK, 1979)
    • (1979) SERC Collaborative Computing Project No. 4 , vol.4
  • 14
    • 0023644992 scopus 로고
    • Refined structure of glutathione reductase at 1.54 Å resolution
    • Karplus, P.A. and Shultz, G.E. (1987) Refined structure of glutathione reductase at 1.54 Å resolution. J. Mol. Biol. 195, 701-729
    • (1987) J. Mol. Biol. , vol.195 , pp. 701-729
    • Karplus, P.A.1    Shultz, G.E.2
  • 16
    • 84967852329 scopus 로고
    • MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
    • Fitzgerald, P.M.D. (1988) MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Cryst. 21, 273-278
    • (1988) J. Appl. Cryst. , vol.21 , pp. 273-278
    • Fitzgerald, P.M.D.1
  • 18
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Cryst. A50, 157-163
    • (1994) Acta Cryst. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 20
    • 0000858864 scopus 로고
    • SQUASH-combining constraints for macromolecular phase refinement and extension
    • Zhang, K.Y.J. (1993) SQUASH-combining constraints for macromolecular phase refinement and extension. Acta Cryst. D49, 213-222
    • (1993) Acta Cryst. , vol.D49 , pp. 213-222
    • Zhang, K.Y.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.