메뉴 건너뛰기




Volumn 217, Issue 12, 2002, Pages 686-693

Towards automated protein structure determination: BnP, the SnB-PHASES interface

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; AUTOMATION; CONFERENCE PAPER; CRYSTALLOGRAPHY; DENSITY; PHASE TRANSITION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0042810719     PISSN: 00442968     EISSN: None     Source Type: Journal    
DOI: 10.1524/zkri.217.12.686.20659     Document Type: Conference Paper
Times cited : (55)

References (36)
  • 1
    • 0034697984 scopus 로고    scopus 로고
    • The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins
    • Alphey, M. S.; Bond, C. S.; Tetaud, E.; Fairlamb, A. H.; Hunter, W. N.: The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins. J. Mol. Biol. 300 (2000) 903-916.
    • (2000) J. Mol. Biol. , vol.300 , pp. 903-916
    • Alphey, M.S.1    Bond, C.S.2    Tetaud, E.3    Fairlamb, A.H.4    Hunter, W.N.5
  • 2
    • 0037161258 scopus 로고    scopus 로고
    • Structure of the pyruvate dehydrogenase multienzyme complex El component from Escherichia coli at 1.85 Å resolution
    • Arjunan, P.; Nemeria, N.; Brunskill, A.; Chandrasekhar, K.; Sax, M.; Yan, Y.; Jordan, F.; Guest, J.; Furey, W.: Structure of the pyruvate dehydrogenase multienzyme complex El component from Escherichia coli at 1.85 Å resolution. Biochemistry 41 (2002) 5213-5221.
    • (2002) Biochemistry , vol.41 , pp. 5213-5221
    • Arjunan, P.1    Nemeria, N.2    Brunskill, A.3    Chandrasekhar, K.4    Sax, M.5    Yan, Y.6    Jordan, F.7    Guest, J.8    Furey, W.9
  • 3
    • 0001453644 scopus 로고
    • The refinement of atomic parameters by direct calculation of the minimum residual
    • Bhuiya, A. K.; Stanley, E.: The refinement of atomic parameters by direct calculation of the minimum residual. Acta Crystallogr. 16 (1963) 981-984.
    • (1963) Acta Crystallogr. , vol.16 , pp. 981-984
    • Bhuiya, A.K.1    Stanley, E.2
  • 4
    • 0001763933 scopus 로고    scopus 로고
    • Difference structure factor normalization for heavy-atom or anomalous scattering substructure determinations
    • Blessing, R. H.; Smith, G. D.: Difference structure factor normalization for heavy-atom or anomalous scattering substructure determinations. J. Appl. Cryst. 32 (1999) 664-670.
    • (1999) J. Appl. Cryst. , vol.32 , pp. 664-670
    • Blessing, R.H.1    Smith, G.D.2
  • 5
    • 0033575671 scopus 로고    scopus 로고
    • The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding
    • Bochkarev, A.; Bochkareva, E.; Frappier, L.; Edwards, A. M.: The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. EMBO J. 18 (1999) 4498-4504.
    • (1999) EMBO J. , vol.18 , pp. 4498-4504
    • Bochkarev, A.1    Bochkareva, E.2    Frappier, L.3    Edwards, A.M.4
  • 6
    • 0004049745 scopus 로고    scopus 로고
    • Sixty-six Se atoms and 2160 amino acids in the asymmetric unit: Structure of AEP-transaminase
    • Abstract 02. 06. 03, St. Paul, MN
    • Chen, C. C. H.; Kim, A.; Zhang, H.; Howard, A. J.; Sheldrick, G.; Dunaway-Mariano, D.; Herzberg, O.: Sixty-six Se atoms and 2160 amino acids in the asymmetric unit: structure of AEP-transaminase. Abstract 02. 06. 03, ACA Annual Meeting, St. Paul, MN (2000).
    • (2000) ACA Annual Meeting
    • Chen, C.C.H.1    Kim, A.2    Zhang, H.3    Howard, A.J.4    Sheldrick, G.5    Dunaway-Mariano, D.6    Herzberg, O.7
  • 7
    • 0000151148 scopus 로고
    • Structure solution by minimal function phase refinement and Fourier filtering: Theoretical basis
    • DeTitta, G. T.; Weeks, C. M.; Thuman, P.; Miller, R.; Hauptman, H. A.: Structure solution by minimal function phase refinement and Fourier filtering: theoretical basis. Acta Crystallogr. A50 (1994) 203-210.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 203-210
    • DeTitta, G.T.1    Weeks, C.M.2    Thuman, P.3    Miller, R.4    Hauptman, H.A.5
  • 8
    • 0032963901 scopus 로고    scopus 로고
    • Ab initio structure solution of a dimeric cytochrome c3 from Desulfovibrio gigas containing disulfide bridges
    • Frazão C.; Sieker, L.; Sheldrick, G. M.; Lamzin, V.; LeGall, J.; Carrondo, M. A.: Ab initio structure solution of a dimeric cytochrome c3 from Desulfovibrio gigas containing disulfide bridges. J. Biol. Inorg. Chem. 4 (1999) 162-165.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 162-165
    • Frazão, C.1    Sieker, L.2    Sheldrick, G.M.3    Lamzin, V.4    LeGall, J.5    Carrondo, M.A.6
  • 9
    • 85055704314 scopus 로고
    • Experiences with a new translation-function program
    • Fujinaga, M.; Read, R. J.: Experiences with a new translation-function program. J. Appl. Cryst. 20 (1987) 517-521.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 517-521
    • Fujinaga, M.1    Read, R.J.2
  • 10
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for processing and analyzing diffraction data from macromolecules
    • Furey, W.; Swaminathan, S.: PHASES-95: a program package for processing and analyzing diffraction data from macromolecules. Meth. Enzymol. 277 (1997) 590-620.
    • (1997) Meth. Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 11
    • 0002793751 scopus 로고
    • On the application of phase relationships to complex structures
    • Germain, G.; Woolfson, M. M.: On the application of phase relationships to complex structures. Acta Crystallogr. B24 (1968) 91-96.
    • (1968) Acta Crystallogr. , vol.B24 , pp. 91-96
    • Germain, G.1    Woolfson, M.M.2
  • 13
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W.: Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254 (1991) 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.1
  • 14
    • 0034161543 scopus 로고    scopus 로고
    • Crystal structure of the catalytic portion of human HMG-CoA reductase: Insights into regulation of activity and catalysis
    • Istvan, E. S.; Palnitkar, M.; Buchanan, S. K.; Deisenhofer, J.: Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. EMBO J. 19 (2000) 819-830.
    • (2000) EMBO J. , vol.19 , pp. 819-830
    • Istvan, E.S.1    Palnitkar, M.2    Buchanan, S.K.3    Deisenhofer, J.4
  • 15
    • 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.; Cowtan, S. W.; Kjeldgaard, M.: Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47 (1991) 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowtan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0002544124 scopus 로고
    • Linear algebraic analyses of structures with one predominant type of anomalous scatterer
    • Karle, J.: Linear algebraic analyses of structures with one predominant type of anomalous scatterer. Acta Crystallogr. A45 (1989) 303-307.
    • (1989) Acta Crystallogr. , vol.A45 , pp. 303-307
    • Karle, J.1
  • 18
    • 0034928937 scopus 로고    scopus 로고
    • Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: A novel enzymatic function on an ancient metal binding scaffold
    • McCarthy, A. A.; Baker, H. M.; Shewry, S. C.; Patchett, M. L.; Baker, E. N.: Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: a novel enzymatic function on an ancient metal binding scaffold. Structure 9 (2001) 637-646.
    • (2001) Structure , vol.9 , pp. 637-646
    • McCarthy, A.A.1    Baker, H.M.2    Shewry, S.C.3    Patchett, M.L.4    Baker, E.N.5
  • 19
    • 0027909076 scopus 로고
    • On the application of the minimal principle to solve unknown structures
    • Miller, R.; DeTitta, G. T.; Jones, R.; Langs, D. A.; Weeks, C. M.; Hauptman, H. A.: On the application of the minimal principle to solve unknown structures. Science 259 (1993) 1430-1433.
    • (1993) Science , vol.259 , pp. 1430-1433
    • Miller, R.1    DeTitta, G.T.2    Jones, R.3    Langs, D.A.4    Weeks, C.M.5    Hauptman, H.A.6
  • 20
    • 0028485498 scopus 로고
    • SnB: Crystal structure determination via Shake-and-Bake
    • Miller, R.; Gallo, S. M.; Khalak, H. G.; Weeks, C. M.: SnB: crystal structure determination via Shake-and-Bake. J. Appl. Cryst. 27 (1994) 613-621.
    • (1994) J. Appl. Cryst. , vol.27 , pp. 613-621
    • Miller, R.1    Gallo, S.M.2    Khalak, H.G.3    Weeks, C.M.4
  • 21
    • 84944815633 scopus 로고
    • The use of MULTAN to locate the positions of anomalous scatterers
    • Mukherjee, A. K.; Helliwell, J. R.; Main, P.: The use of MULTAN to locate the positions of anomalous scatterers. Acta Crystallogr. A45 (1989) 715-718.
    • (1989) Acta Crystallogr. , vol.A45 , pp. 715-718
    • Mukherjee, A.K.1    Helliwell, J.R.2    Main, P.3
  • 22
    • 0036086916 scopus 로고    scopus 로고
    • SnB version 2.2: An example of crystallographic multiprocessing
    • Rappleye, J.; Innus, M.; Weeks, C. M.; Miller, R.: SnB version 2.2: an example of crystallographic multiprocessing. J. Appl. Cryst. 35 (2002) 374-376.
    • (2002) J. Appl. Cryst. , vol.35 , pp. 374-376
    • Rappleye, J.1    Innus, M.2    Weeks, C.M.3    Miller, R.4
  • 23
    • 0002008141 scopus 로고
    • Determination of phases by the conditions of non-crystallographic symmetry
    • Rossmann, M. G.; Blow, D. M.: Determination of phases by the conditions of non-crystallographic symmetry. Acta Crystallogr. 16 (1963) 39-44.
    • (1963) Acta Crystallogr. , vol.16 , pp. 39-44
    • Rossmann, M.G.1    Blow, D.M.2
  • 24
  • 27
    • 0036080068 scopus 로고    scopus 로고
    • Matching selenium-atom peak positions with a different hand or origin
    • Smith, G. D.: Matching selenium-atom peak positions with a different hand or origin. J. Appl. Cryst. 35 (2002) 368-370.
    • (2002) J. Appl. Cryst. , vol.35 , pp. 368-370
    • Smith, G.D.1
  • 28
    • 0033081959 scopus 로고    scopus 로고
    • Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methods
    • Terwilliger, T. C.; Berendzen, J.: Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methods. Acta Crystallogr. D55 (1999) 501-505.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 501-505
    • Terwilliger, T.C.1    Berendzen, J.2
  • 30
    • 0042541638 scopus 로고    scopus 로고
    • The 160 selenium atom substructure of KPHMT
    • von Delft, F.; Blundell, T. L.: The 160 selenium atom substructure of KPHMT. Acta. Crystallogr. A58 (Supplement) (2002) C239.
    • (2002) Acta. Crystallogr. , vol.A58 , Issue.SUPPL.
    • Von Delft, F.1    Blundell, T.L.2
  • 31
    • 0022325950 scopus 로고
    • Solvent flattening
    • Wang, B.-C.: Solvent flattening. Meth. Enzymol. 115 (1985) 90-112.
    • (1985) Meth. Enzymol. , vol.115 , pp. 90-112
    • Wang, B.-C.1
  • 32
    • 0000257188 scopus 로고
    • Structure solution by minimal function phase refinement and Fourier filtering: II. Implementation and applications
    • Weeks, C. M.; DeTitta, G. T.; Hauptman, H. A.; Thuman, P.; Miller, R.: Structure solution by minimal function phase refinement and Fourier filtering: II. implementation and applications. Acta Crystallogr. A50 (1994) 210-220.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 210-220
    • Weeks, C.M.1    DeTitta, G.T.2    Hauptman, H.A.3    Thuman, P.4    Miller, R.5
  • 33
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks, C. M.; Miller, R.: The design and implementation of SnB v2.0. J. Appl. Cryst. 32 (1999) 120-124.
    • (1999) J. Appl. Cryst. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 34
    • 0005944336 scopus 로고    scopus 로고
    • Ab initio phasing by dual-space direct methods
    • (R. Kužel and J. Hašek, eds.), Czech and Slovak Cryst. Assn., Praha
    • Weeks, C. M.; Sheldrick, G. M.; Miller, R.; Usón, I.; Hauptman, H. A.: Ab initio phasing by dual-space direct methods. In Advances in Structure Analysis (R. Kužel and J. Hašek, eds.), Czech and Slovak Cryst. Assn., Praha (2001) 37-64.
    • (2001) Advances in Structure Analysis , pp. 37-64
    • Weeks, C.M.1    Sheldrick, G.M.2    Miller, R.3    Usón, I.4    Hauptman, H.A.5
  • 35
    • 0000897766 scopus 로고
    • The application of MULTAN to the analysis of isomorphous derivatives in protein crystallography
    • Wilson, K. S.: The application of MULTAN to the analysis of isomorphous derivatives in protein crystallography. Acta Crystallogr. B34 (1978) 1599-1608.
    • (1978) Acta Crystallogr. , vol.B34 , pp. 1599-1608
    • Wilson, K.S.1
  • 36
    • 0033566912 scopus 로고    scopus 로고
    • +-dependent malic enzyme: A new class of oxidative decarboxylases
    • +-dependent malic enzyme: a new class of oxidative decarboxylases. Structure 7 (1999) 877-889.
    • (1999) Structure , vol.7 , pp. 877-889
    • Xu, Y.1    Bhargava, G.2    Wu, H.3    Loeber, G.4    Tong, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.