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Volumn 3, Issue 1-2, 2002, Pages 25-32

Establishing a structural genomics platform: The Berlin-based protein structure factory

Author keywords

High throughput; NMR spectroscopy; Protein structure analysis; Structural genomics proteomics; X ray crystallography

Indexed keywords

COMPLEMENTARY DNA; LIGAND; PROTEIN;

EID: 0036408370     PISSN: 14387506     EISSN: None     Source Type: Journal    
DOI: 10.1002/1438-826X(200210)3:1/2<25::AID-GNFD25>3.0.CO;2-W     Document Type: Short Survey
Times cited : (6)

References (86)
  • 1
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • International Human Genome Sequencing Consortium (2001) Initial sequencing and analysis of the human genome. Nature 409: 860-921.
    • (2001) Nature , vol.409 , pp. 860-921
  • 2
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J. C. et al. (2001) The sequence of the human genome. Science 291: 1304-1351.
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 4
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell, T. L., Jhoti, H., Abell, C. (2002) High-throughput crystallography for lead discovery in drug design. Nature Rev. Drug Discov. 1: 45-54.
    • (2002) Nature Rev. Drug Discov. , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 5
    • 0035424346 scopus 로고    scopus 로고
    • High-throughput three-dimensional protein structure determination
    • Heinemann, U., Illing, G., Oschkinat, H. (2001) High-throughput three-dimensional protein structure determination. Curr. Op. Biotechnol. 12: 348-354.
    • (2001) Curr. Op. Biotechnol. , vol.12 , pp. 348-354
    • Heinemann, U.1    Illing, G.2    Oschkinat, H.3
  • 6
    • 0002822987 scopus 로고    scopus 로고
    • High-throughput structural proteomics using x-rays
    • Jhoti, H. (2001) High-throughput structural proteomics using x-rays. Trends Biotechnol. 19: 67-71.
    • (2001) Trends Biotechnol. , vol.19 , pp. 67-71
    • Jhoti, H.1
  • 7
    • 0033762983 scopus 로고    scopus 로고
    • Current state of automated crystallographic data analysis
    • Lamzin, V. S., Perrakis, A. (2000) Current state of automated crystallographic data analysis. Nature Struct. Biol. 7: 978-981.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 978-981
    • Lamzin, V.S.1    Perrakis, A.2
  • 8
    • 0033638111 scopus 로고    scopus 로고
    • An approach for high-throughput structure determination of proteins by NMR spectroscopy
    • Medek, A., Olejniczak, E. T., Meadows, R. P., Fesik, S. W. (2000) An approach for high-throughput structure determination of proteins by NMR spectroscopy. J. Biomol. NMR 18: 229-238.
    • (2000) J. Biomol. NMR , vol.18 , pp. 229-238
    • Medek, A.1    Olejniczak, E.T.2    Meadows, R.P.3    Fesik, S.W.4
  • 10
    • 0032857781 scopus 로고    scopus 로고
    • Automated analysis of NMR assignments and structures for proteins
    • Moseley, H. N., Montelione, G. T. (1999) Automated analysis of NMR assignments and structures for proteins. Curr. Op. Struct. Biol. 9: 635-642.
    • (1999) Curr. Op. Struct. Biol. , vol.9 , pp. 635-642
    • Moseley, H.N.1    Montelione, G.T.2
  • 11
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins. EMBO J. 5: 823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 12
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo, C. A., Jones, D. T., Thornton, J. M. (1994) Protein superfamilies and domain superfolds. Nature 372: 631-634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 17
    • 0344109574 scopus 로고    scopus 로고
    • Structural genomics taking shape
    • Gaasterland, T. (1998) Structural genomics taking shape. Trends Genet. 14: 135.
    • (1998) Trends Genet. , vol.14 , pp. 135
    • Gaasterland, T.1
  • 18
    • 0032102671 scopus 로고    scopus 로고
    • Beyond complete genomes: From sequence to structure and function
    • Koonin, E. V., Tatusov, R. L., Galperin, M. Y. (1998) Beyond complete genomes: From sequence to structure and function. Curr. Op. Struct. Biol. 8: 355-363.
    • (1998) Curr. Op. Struct. Biol. , vol.8 , pp. 355-363
    • Koonin, E.V.1    Tatusov, R.L.2    Galperin, M.Y.3
  • 19
    • 0032921818 scopus 로고    scopus 로고
    • Structural genomics: Keystone for a Human Proteome Project
    • Montelione, G. T., Anderson, S. (1999) Structural genomics: Keystone for a Human Proteome Project. Nature Struct. Biol. 6: 11-12.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 11-12
    • Montelione, G.T.1    Anderson, S.2
  • 20
    • 0031787022 scopus 로고    scopus 로고
    • 100,000 Protein structures for the biologist
    • Šali, A. (1998) 100,000 protein structures for the biologist. Nature Struct. Biol. 5: 1029-1032.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1029-1032
    • Šali, A.1
  • 21
    • 0032521199 scopus 로고    scopus 로고
    • The Argonne Structural Genomics Workshop: Lamaze class for the birth of a new science
    • Shapiro, L., Lima, C. D. (1998) The Argonne Structural Genomics Workshop: Lamaze class for the birth of a new science. Structure 6: 265-267.
    • (1998) Structure , vol.6 , pp. 265-267
    • Shapiro, L.1    Lima, C.D.2
  • 22
    • 0031665755 scopus 로고    scopus 로고
    • Class-directed structure determination: Foundation for a protein structure initiative
    • Terwilliger, T. C., Waldo, G., Peat, T. S., Newman, J. M., Chu, K., Berendzen, J. (1998) Class-directed structure determination: Foundation for a protein structure initiative. Protein Sci. 7: 1851-1856.
    • (1998) Protein Sci. , vol.7 , pp. 1851-1856
    • Terwilliger, T.C.1    Waldo, G.2    Peat, T.S.3    Newman, J.M.4    Chu, K.5    Berendzen, J.6
  • 24
    • 0033757822 scopus 로고    scopus 로고
    • An overview of structural genomics
    • Burley, S.K. (2000) An overview of structural genomics. Nature Struct. Biol. 7: 932-934.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 932-934
    • Burley, S.K.1
  • 25
    • 0033757915 scopus 로고    scopus 로고
    • Structural genomics in Europe: Slow start, strong finish?
    • Heinemann, U. (2000) Structural genomics in Europe: Slow start, strong finish? Nature Struct. Biol. 7: 940-942.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 940-942
    • Heinemann, U.1
  • 26
    • 0033757870 scopus 로고    scopus 로고
    • Structural genomics in North America
    • Terwilliger, T.C. (2000) Structural genomics in North America. Nature Struct. Biol. 7: 935-939.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 935-939
    • Terwilliger, T.C.1
  • 28
    • 0035812704 scopus 로고    scopus 로고
    • Global efforts in structural genomics
    • Stevens, R. C., Yokoyama, S., Wilson, I. A. (2001) Global efforts in structural genomics. Science 294: 89-92.
    • (2001) Science , vol.294 , pp. 89-92
    • Stevens, R.C.1    Yokoyama, S.2    Wilson, I.A.3
  • 30
    • 0033768266 scopus 로고    scopus 로고
    • Target selection for structural genomics
    • Brenner, S. E. (2000) Target selection for structural genomics. Nature Struct. Biol. 7: 967-969.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 967-969
    • Brenner, S.E.1
  • 31
    • 0033730342 scopus 로고    scopus 로고
    • Methodologies for target selection in structural genomics
    • Linial, M., Yona, G. (2000) Methodologies for target selection in structural genomics. Prog. Biophys. Mol. Biol. 73: 297-320.
    • (2000) Prog. Biophys. Mol. Biol. , vol.73 , pp. 297-320
    • Linial, M.1    Yona, G.2
  • 32
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent
    • Hochuli, E., Bannwarth, W., Dobeli, H., Gentz, R., Stüber, D. (1988) Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. Biotechnology 6: 1321-1325.
    • (1988) Biotechnology , vol.6 , pp. 1321-1325
    • Hochuli, E.1    Bannwarth, W.2    Dobeli, H.3    Gentz, R.4    Stüber, D.5
  • 33
    • 0033624216 scopus 로고    scopus 로고
    • Automated purification of His6-tagged proteins allows exhaustive screening of libraries generated by random mutagenesis
    • Lanio, T., Jeltsch, A., Pingoud, A. (2000) Automated purification of His6-tagged proteins allows exhaustive screening of libraries generated by random mutagenesis. Biotechniques 29: 338-342.
    • (2000) Biotechniques , vol.29 , pp. 338-342
    • Lanio, T.1    Jeltsch, A.2    Pingoud, A.3
  • 34
    • 0027991404 scopus 로고
    • One-step affinity purification of bacterially produced proteins by means of the "Strep-tag" and immobilized recombinant core streptavidin
    • Schmidt, T. G. M., Skerra, A. (1994) One-step affinity purification of bacterially produced proteins by means of the "Strep-tag" and immobilized recombinant core streptavidin. J. Chromatogr. A 676: 337-345.
    • (1994) J. Chromatogr. A , vol.676 , pp. 337-345
    • Schmidt, T.G.M.1    Skerra, A.2
  • 36
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • Lilie, H., Schwarz, E., Rudolph, R. (1998) Advances in refolding of proteins produced in E. coli. Curr. Op. Biotechnol. 9: 497-501.
    • (1998) Curr. Op. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 37
    • 0034999062 scopus 로고    scopus 로고
    • Folding screening assayed by proteolysis: Application to various cystine deletion mutants of vascular endothelial growth factor
    • Heiring, C., Muller, Y. A. (2001) Folding screening assayed by proteolysis: Application to various cystine deletion mutants of vascular endothelial growth factor. Protein Engng. 14: 183-188.
    • (2001) Protein Engng. , vol.14 , pp. 183-188
    • Heiring, C.1    Muller, Y.A.2
  • 38
    • 0035222401 scopus 로고    scopus 로고
    • The Berlin "Protein structure factory" initiative: A technology-oriented approach to structural genomics
    • (Schlichting, I., Egner, U., Eds.). Berlin, Heidelberg, New York: Springer Verlag
    • Heinemann, U. (2001) The Berlin "Protein Structure Factory" initiative: A technology-oriented approach to structural genomics, in: Data Mining in Structural Biology: Signal Transduction and Beyond (Schlichting, I., Egner, U., Eds.) pp. 101-121, Berlin, Heidelberg, New York: Springer Verlag.
    • (2001) Data Mining in Structural Biology: Signal Transduction and Beyond , pp. 101-121
    • Heinemann, U.1
  • 39
    • 0011147706 scopus 로고    scopus 로고
    • Linking structural biology with genome research: The Berlin "Protein Structure Factory" initiative
    • (Suhai, S., Ed.). New York: Kluwer Academic/Plenum Publ
    • Heinemann, U., Frevert, J., Hofmann, K. P., Illing, G., Oschkinat, H., Saenger, W., Zettl, R. (2000) Linking structural biology with genome research: The Berlin "Protein Structure Factory" initiative, in: Genomics and Proteomics (Suhai, S., Ed.) pp. 179-189, New York: Kluwer Academic/Plenum Publ.
    • (2000) Genomics and Proteomics , pp. 179-189
    • Heinemann, U.1    Frevert, J.2    Hofmann, K.P.3    Illing, G.4    Oschkinat, H.5    Saenger, W.6    Zettl, R.7
  • 43
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., VanDyke, M., Stock, J. (1991) Predicting coiled coils from protein sequences. Science 252: 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    VanDyke, M.2    Stock, J.3
  • 44
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequences
    • Wootton, J. C., Federhen, S. (1996) Analysis of compositionally biased regions in sequences. Methods Enzymol. 266: 554-571.
    • (1996) Methods Enzymol. , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2
  • 45
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane α-helices in prokaryotic membrane proteins: The Dense Alignment Surface method
    • Cserzö, M., Wallin, E., Simon, I., von Heijne, G., Elofsson, A. (1997) Prediction of transmembrane α-helices in prokaryotic membrane proteins: The Dense Alignment Surface method. Protein Engng. 10: 673-676.
    • (1997) Protein Engng. , vol.10 , pp. 673-676
    • Cserzö, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 46
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: A historical perspective
    • Drews, J. (2000) Drug discovery: A historical perspective. Science 287: 1960-1964.
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 47
  • 48
    • 0035157217 scopus 로고    scopus 로고
    • Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II
    • Bushnell, D. A., Cramer, P., Kornberg, R. D. (2001) Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II. Structure 9: R11-R14.
    • (2001) Structure , vol.9
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 49
    • 0025262173 scopus 로고
    • Selenomethionyl-proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W. A., Horton, J. R., LeMaster, D. M. (1990) Selenomethionyl-proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J. 9: 1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 50
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto, N. K., Kay, L. E. (2000) New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Op. Struct. Biol. 10: 585-592.
    • (2000) Curr. Op. Struct. Biol. , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 52
  • 53
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M. (1993) Procheck: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 54
    • 0032493714 scopus 로고    scopus 로고
    • Quality assessment of NMR structures: A statistical survey
    • Doreleijers, J. F., Rullmann, J. A. C., Kaptein, R. (1998) Quality assessment of NMR structures: A statistical survey. J. Mol. Biol. 281: 149-164.
    • (1998) J. Mol. Biol. , vol.281 , pp. 149-164
    • Doreleijers, J.F.1    Rullmann, J.A.C.2    Kaptein, R.3
  • 56
    • 0032896079 scopus 로고    scopus 로고
    • Difference density quality (DDQ): A method to assess the global and local correctness of macromolecular crystal structures
    • van den Akker, F., Hol, W. G. J. (1999) Difference density quality (DDQ): A method to assess the global and local correctness of macromolecular crystal structures. Acta Crystallogr. D 55: 206-218.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 206-218
    • Van den Akker, F.1    Hol, W.G.J.2
  • 57
    • 0032526959 scopus 로고    scopus 로고
    • Validation tools: Can they indicate the information content of macromolecular crystal structures?
    • Dodson, E. J., Davies, G. J., Lamzin, V. S., Murshudov, G. N., Wilson, K. S. (1998) Validation tools: Can they indicate the information content of macromolecular crystal structures? Structure 6: 685-690.
    • (1998) Structure , vol.6 , pp. 685-690
    • Dodson, E.J.1    Davies, G.J.2    Lamzin, V.S.3    Murshudov, G.N.4    Wilson, K.S.5
  • 58
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A. A., Richelle, J., Wodak, S. J. (1999) SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D 55: 191-205.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 59
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P., Fesik, S. W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science 274: 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 60
    • 0032212208 scopus 로고    scopus 로고
    • A method for global protein expression and antibody screening on high-density filters of an arrayed cDNA library
    • Büssow, K., Cahill, D., Nietfeld, W., Bancroft, D. R., Scherzinger, E., Lehrach, H., Walter, G. (1998) A method for global protein expression and antibody screening on high-density filters of an arrayed cDNA library. Nucleic Acids Res. 26: 5007-5008.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5007-5008
    • Büssow, K.1    Cahill, D.2    Nietfeld, W.3    Bancroft, D.R.4    Scherzinger, E.5    Lehrach, H.6    Walter, G.7
  • 61
    • 0030862012 scopus 로고    scopus 로고
    • Automated array technologies for gene expression profiling
    • Maier, E., Maier-Ewert, S., Lehrach, H. (1997) Automated array technologies for gene expression profiling. Drug Discov. Today 2: 315-324.
    • (1997) Drug Discov. Today , vol.2 , pp. 315-324
    • Maier, E.1    Maier-Ewert, S.2    Lehrach, H.3
  • 62
    • 0032247126 scopus 로고    scopus 로고
    • Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY
    • Koradi, R., Billeter, M., Engeli, M., Güntert, P., Wüthrich, K. (1998) Automated peak picking and peak integration in macromolecular NMR spectra using AUTOPSY. J. Magn. Reson. 135: 288-297.
    • (1998) J. Magn. Reson. , vol.135 , pp. 288-297
    • Koradi, R.1    Billeter, M.2    Engeli, M.3    Güntert, P.4    Wüthrich, K.5
  • 63
    • 0035744168 scopus 로고    scopus 로고
    • Automatic assignment of NOESY cross peaks and determination of the protein structure of a new world scorpion neurotoxin using NOAH/DIAMOND
    • Xu, Y., Jablonsky, M. J., Jackson, P. L., Braun, W., Krishna, N. R. (2001) Automatic assignment of NOESY cross peaks and determination of the protein structure of a new world scorpion neurotoxin using NOAH/DIAMOND. J. Magn. Reson. 148: 35-46.
    • (2001) J. Magn. Reson. , vol.148 , pp. 35-46
    • Xu, Y.1    Jablonsky, M.J.2    Jackson, P.L.3    Braun, W.4    Krishna, N.R.5
  • 64
    • 0034501067 scopus 로고    scopus 로고
    • De novo protein structure determination using sparse NMR data
    • Bowers, P. M., Strauss, C. E., Baker, D. (2000) De novo protein structure determination using sparse NMR data. J. Biomol. NMR 18: 311-318.
    • (2000) J. Biomol. NMR , vol.18 , pp. 311-318
    • Bowers, P.M.1    Strauss, C.E.2    Baker, D.3
  • 65
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13: 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 66
    • 0034388123 scopus 로고    scopus 로고
    • Rapid determination of protein folds using residual dipolar couplings
    • Fowler, C. A., Tian, F., Al-Hashimi, H. M., Prestegard, J. H. (2000) Rapid determination of protein folds using residual dipolar couplings. J. Mol. Biol. 304: 447-460.
    • (2000) J. Mol. Biol. , vol.304 , pp. 447-460
    • Fowler, C.A.1    Tian, F.2    Al-Hashimi, H.M.3    Prestegard, J.H.4
  • 67
    • 0033811768 scopus 로고    scopus 로고
    • DipoCoup: A versatile program for 3D-structure homology comparison based on residual dipolar couplings and pseudocontact shifts
    • Meiler, J., Peti, W., Griesinger, C. (2000) DipoCoup: A versatile program for 3D-structure homology comparison based on residual dipolar couplings and pseudocontact shifts. J. Biomol. NMR 17: 283-294.
    • (2000) J. Biomol. NMR , vol.17 , pp. 283-294
    • Meiler, J.1    Peti, W.2    Griesinger, C.3
  • 68
    • 0034306122 scopus 로고    scopus 로고
    • TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
    • Riek, R., Pervushin, K., Wüthrich, K. (2000) TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem. Sci. 25: 462-468.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 462-468
    • Riek, R.1    Pervushin, K.2    Wüthrich, K.3
  • 69
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges, M., Macias, M. C., O'Donoghue, S. I., Oschkinat, H. (1997) Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J. Mol. Biol. 269: 408-422.
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.C.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 71
    • 0035121745 scopus 로고    scopus 로고
    • Practical experience with the use of halides for phasing macromolecular structures: A powerful tool for structural genomics
    • Dauter, Z., Li, M., Wlodawer, A. (2001) Practical experience with the use of halides for phasing macromolecular structures: A powerful tool for structural genomics. Acta Crystallogr. D 57: 239-249.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 239-249
    • Dauter, Z.1    Li, M.2    Wlodawer, A.3
  • 72
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • Hendrickson, W. A., Ogata, C. M. (1997) Phase determination from multiwavelength anomalous diffraction measurements. Methods Enzymol. 276: 494-523.
    • (1997) Methods Enzymol. , vol.276 , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 73
    • 0033732707 scopus 로고    scopus 로고
    • Singlewavelength anomalous diffraction phasing revisited
    • Rice, L. M., Earnest, T. N., Brunger, A. T. (2000) Singlewavelength anomalous diffraction phasing revisited. Acta Crystallogr. D 56: 1413-1420.
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1413-1420
    • Rice, L.M.1    Earnest, T.N.2    Brunger, A.T.3
  • 74
    • 0031045817 scopus 로고    scopus 로고
    • Overview of synchrotron radiation and macromolecular crystallography
    • Helliwell, J. R. (1997) Overview of synchrotron radiation and macromolecular crystallography. Methods Enzymol. 276: 203-217.
    • (1997) Methods Enzymol. , vol.276 , pp. 203-217
    • Helliwell, J.R.1
  • 76
    • 0032167987 scopus 로고    scopus 로고
    • Integrated software for a macromolecular crystallography synchrotron beamline
    • Skinner, J. M., Sweet, R. M. (1998) Integrated software for a macromolecular crystallography synchrotron beamline. Acta Crystallogr. D 54: 718-725.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 718-725
    • Skinner, J.M.1    Sweet, R.M.2
  • 78
    • 0033081529 scopus 로고    scopus 로고
    • Rapid automated molecular replacement by evolutionary search
    • Kissinger, C. R., Gehlhaar, D. K., Fogel, D. B. (1999) Rapid automated molecular replacement by evolutionary search. Acta Crystallogr. D 55: 484-491.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 484-491
    • Kissinger, C.R.1    Gehlhaar, D.K.2    Fogel, D.B.3
  • 79
    • 0033199044 scopus 로고    scopus 로고
    • A highly automated heavy-atom search procedure for macromolecular structures
    • Grosse-Kunstleve, R. W., Brunger, A. T. (1999) A highly automated heavy-atom search procedure for macromolecular structures. Acta Crystallogr. D 55: 1568-1577.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1568-1577
    • Grosse-Kunstleve, R.W.1    Brunger, A.T.2
  • 80
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T. C., Berendzen, J. (1999) Automated structure solution for MIR and MAD. Acta Crystallogr. D 55: 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 81
    • 0032806795 scopus 로고    scopus 로고
    • A database method for automated map interpretation in protein crystallography
    • Diller, D. J., Redinbo, M. R., Pohl, E., Hol, W. G. (1999) A database method for automated map interpretation in protein crystallography. Proteins: Struct. Funct. Genet. 36: 526-541.
    • (1999) Proteins: Struct. Funct. Genet. , vol.36 , pp. 526-541
    • Diller, D.J.1    Redinbo, M.R.2    Pohl, E.3    Hol, W.G.4
  • 82
    • 0034082169 scopus 로고    scopus 로고
    • Determining protein structure from electron-density maps using pattern matching
    • Holton, T., Ioerger, T. R., Christopher, J. A., Sacchettini, J. C. (2000) Determining protein structure from electron-density maps using pattern matching. Acta Crystallogr. D. 56: 722-734.
    • (2000) Acta Crystallogr. D , vol.56 , pp. 722-734
    • Holton, T.1    Ioerger, T.R.2    Christopher, J.A.3    Sacchettini, J.C.4
  • 83
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6: 458-463.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.