메뉴 건너뛰기




Volumn 4, Issue 8, 1996, Pages 897-904

Checking your imagination: Applications of the free R value

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0030586823     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00097-4     Document Type: Article
Times cited : (367)

References (39)
  • 1
    • 0001644632 scopus 로고
    • Between objectivity and subjectivity
    • Brändén, C.I. & Jones, TA (1990). Between objectivity and subjectivity. Nature 343, 687-689.
    • (1990) Nature , vol.343 , pp. 687-689
    • Brändén, C.I.1    Jones, T.A.2
  • 2
    • 0011221526 scopus 로고    scopus 로고
    • Good model-building and refinement practice
    • in press
    • Kleywegt, G.J. & Jones, T.A. (1996). Good model-building and refinement practice. Methods Enzymol., in press.
    • (1996) Methods Enzymol.
    • Kleywegt, G.J.1    Jones, T.A.2
  • 3
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R-value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 4
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross-validation: The free R-value. Methods and applications
    • Brünger, A.T. (1993). Assessment of phase accuracy by cross-validation: the free R-value. Methods and applications. Acta Cryst. D 49, 24-36.
    • (1993) Acta Cryst. D , vol.49 , pp. 24-36
    • Brünger, A.T.1
  • 5
    • 16044370755 scopus 로고    scopus 로고
    • The free R-value: A more objective statistic for crystallography
    • in press
    • Brünger, A.T. (1996). The free R-value: a more objective statistic for crystallography. Methods Enzymol. in press.
    • (1996) Methods Enzymol.
    • Brünger, A.T.1
  • 6
    • 84944818276 scopus 로고
    • Maximum entropy and the foundations of direct methods
    • Bricogne, G. (1984). Maximum entropy and the foundations of direct methods. Acta Cryst. A 40, 410-445.
    • (1984) Acta Cryst. A , vol.40 , pp. 410-445
    • Bricogne, G.1
  • 7
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • in press
    • Pannu, N.S. & Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Cryst. A 52, in press.
    • (1996) Acta Cryst. A , vol.52
    • Pannu, N.S.1    Read, R.J.2
  • 8
    • 84977303434 scopus 로고
    • R-free likelihood-based estimates of errors for phases calculated from atomic models
    • Lunin, V.Yu. & Skovoroda, T.P. (1995). R-free likelihood-based estimates of errors for phases calculated from atomic models. Acta Cryst. A 51, 880-887.
    • (1995) Acta Cryst. A , vol.51 , pp. 880-887
    • Lunin, V.Yu.1    Skovoroda, T.P.2
  • 10
    • 0026801565 scopus 로고
    • Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0 A resolution
    • Curmi, P.M., Schreuder, H., Cascio, D., Sweet, R.M. & Eisenberg, D. (1992). Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0 A resolution. J. Biol. Chem. 267, 16980-16989.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16980-16989
    • Curmi, P.M.1    Schreuder, H.2    Cascio, D.3    Sweet, R.M.4    Eisenberg, D.5
  • 11
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt, G.J., et al., & Jones, T.A. (1994). Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 2, 1241-1258.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Jones, T.A.2
  • 12
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • Kleywegt, G.J. & Jones, T.A. (1995). Where freedom is given, liberties are taken. Structure 3, 535-540.
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2
  • 13
    • 0008840364 scopus 로고
    • Braille for pugilists
    • Hunter, W.N., Thornton, J.M. & Bailey, S., eds, SERC Daresbury Laboratory, Warrington, UK
    • Kleywegt, G.J. & Jones, T.A. (1995). Braille for pugilists. In Making the Most of Your Model. (Hunter, W.N., Thornton, J.M. & Bailey, S., eds), pp. 11-24, SERC Daresbury Laboratory, Warrington, UK.
    • (1995) Making the Most of Your Model , pp. 11-24
    • Kleywegt, G.J.1    Jones, T.A.2
  • 14
    • 0001388361 scopus 로고
    • Largest likely values for the reliability index
    • Wilson, A.J.C. (1950). Largest likely values for the reliability index. Acta Cryst. 3, 397-398.
    • (1950) Acta Cryst. , vol.3 , pp. 397-398
    • Wilson, A.J.C.1
  • 15
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, A.T., Krukowski, A. & Erickson, J.W. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A 46, 585-593.
    • (1990) Acta Cryst. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.W.3
  • 16
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson, A.E., Kleywegt, G.J., Uhlén, M. & Jones, T.A. (1995). Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3, 265-278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhlén, M.3    Jones, T.A.4
  • 17
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 18
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to a 1.5 A resolution structure of crambin
    • Brünger, A.T., Karplus, M. & Petsko, G.A. (1989). Crystallographic refinement by simulated annealing: application to a 1.5 A resolution structure of crambin. Acta Cryst. A 45, 50-61.
    • (1989) Acta Cryst. A , vol.45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 19
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt, G.J. (1996). Use of non-crystallographic symmetry in protein structure refinement. Acta Cryst. D 52, 842-857.
    • (1996) Acta Cryst. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 20
    • 0028885711 scopus 로고
    • Conformational variability in the refined crystal structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig, K., Adams, P.D. & Brünger, A.T. (1995). Conformational variability in the refined crystal structure of the chaperonin GroEL at 2.8 Å resolution. Nat. Struct. Biol. 2, 1083-1094.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 22
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952). Traitement statistique des erreurs dans la determination des structures cristallines. Acta Cryst. 5, 802-810.
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 23
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 24
    • 0017581877 scopus 로고
    • Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin
    • Hsu, I.N., Delbaere, L.T.J., James, M.N.G. & Hoffman, T. (1977). Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin. Nature 266, 140-145.
    • (1977) Nature , vol.266 , pp. 140-145
    • Hsu, I.N.1    Delbaere, L.T.J.2    James, M.N.G.3    Hoffman, T.4
  • 25
    • 85005537029 scopus 로고
    • Thermal motion and conformational disorder in protein crystal structures: Comparison of multi-conformer and time-averaging models
    • Burling, F.T. & Brünger, A.T. (1994). Thermal motion and conformational disorder in protein crystal structures: comparison of multi-conformer and time-averaging models, Isr. J. Chem. 34, 165-175.
    • (1994) Isr. J. Chem. , vol.34 , pp. 165-175
    • Burling, F.T.1    Brünger, A.T.2
  • 26
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J.S. & Brünger, A.T. (1994). Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brünger, A.T.2
  • 27
    • 0001478871 scopus 로고
    • PRISM: Topologically restrained phase refinement for macromolecular crystallography
    • Baker, D., Bystroff, C., Fletterick, R.J. & Agard, D.A. (1993). PRISM: topologically restrained phase refinement for macromolecular crystallography. Acta Cryst. D 49, 429-439.
    • (1993) Acta Cryst. D , vol.49 , pp. 429-439
    • Baker, D.1    Bystroff, C.2    Fletterick, R.J.3    Agard, D.A.4
  • 28
    • 0009482248 scopus 로고
    • Use of the free R-factor as a guide in parameter optimisation for density modification
    • Bailey, S., Hubbard, R. & Waller, D., eds, SERC Daresbury Laboratory, Warrington, UK
    • Grimes, J. & Stuart, D. (1994). Use of the free R-factor as a guide in parameter optimisation for density modification. In From First Map to Final Model. (Bailey, S., Hubbard, R. & Waller, D., eds), pp. 67-76, SERC Daresbury Laboratory, Warrington, UK.
    • (1994) From First Map to Final Model , pp. 67-76
    • Grimes, J.1    Stuart, D.2
  • 29
    • 0029188074 scopus 로고
    • Phase improvement by cross-validated solvent flattening
    • Roberts, A.L.U. & Brünger, A.T. (1995). Phase improvement by cross-validated solvent flattening. Acta Cryst. D 51, 990-1002.
    • (1995) Acta Cryst. D , vol.51 , pp. 990-1002
    • Roberts, A.L.U.1    Brünger, A.T.2
  • 30
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross-validation in iterated density-modification procedures
    • Cowtan, K.D. & Main, P. (1996). Phase combination and cross-validation in iterated density-modification procedures. Acta Cryst. D 52, 43-48.
    • (1996) Acta Cryst. D , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 31
    • 0002660809 scopus 로고
    • The detection of sub-units within the asymmetric unit
    • Rossmann, M.G. & Blow, D.M. (1962). The detection of sub-units within the asymmetric unit. Acta Cryst. 15, 24-31.
    • (1962) Acta Cryst. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 32
    • 0030512814 scopus 로고    scopus 로고
    • A re-evaluation of the crystal structure of chloromuconate cycloisomerase
    • Kleywegt, G.J., Hoier, H. & Jones, T.A. (1996). A re-evaluation of the crystal structure of chloromuconate cycloisomerase. Acta Cryst. D 52, 858-863.
    • (1996) Acta Cryst. D , vol.52 , pp. 858-863
    • Kleywegt, G.J.1    Hoier, H.2    Jones, T.A.3
  • 33
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat proteinoperator complex
    • Valegård, K., Murray, J.B., Stockley, P.G., Stonehouse, N.J. & Liljas, L. (1994). Crystal structure of an RNA bacteriophage coat proteinoperator complex. Nature 371, 623-626.
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegård, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 34
    • 0030022569 scopus 로고    scopus 로고
    • Report of a workshop on the use of statistical validators in protein X-ray crystallography
    • Dodson, E.J., Kleywegt, G.J. & Wilson, K.S. (1996). Report of a workshop on the use of statistical validators in protein X-ray crystallography. Acta Cryst. D 52, 228-234.
    • (1996) Acta Cryst. D , vol.52 , pp. 228-234
    • Dodson, E.J.1    Kleywegt, G.J.2    Wilson, K.S.3
  • 36
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN - Programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection datasets
    • Kleywegt, G.J. & Jones, T.A. (1996). xdlMAPMAN and xdlDATAMAN - programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection datasets. Acta Cryst. D 52, 826-828.
    • (1996) Acta Cryst. D , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 37
    • 0000651098 scopus 로고
    • A real-space refinement procedure for proteins
    • Diamond, R. (1971). A real-space refinement procedure for proteins. Acta Cryst. A 27, 436-452.
    • (1971) Acta Cryst. A , vol.27 , pp. 436-452
    • Diamond, R.1
  • 38
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 39
    • 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. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.