메뉴 건너뛰기




Volumn 397, Issue 3, 2010, Pages 647-663

Crystal Structure of the First Eubacterial Mre11 Nuclease Reveals Novel Features that May Discriminate Substrates During DNA Repair

(47)  Das, Debanu a,b   Moiani, Davide c   Axelrod, Herbert L a,b   Miller, Mitchell D a,b   McMullan, Daniel a,d   Jin, Kevin K a,b   Abdubek, Polat a,d   Astakhova, Tamara a,e   Burra, Prasad a,f   Carlton, Dennis a,c   Chiu, Hsiu Ju a,b   Clayton, Thomas a,c   Deller, Marc C a,c   Duan, Lian a,e   Ernst, Dustin a,d   Feuerhelm, Julie a,d   Grant, Joanna C a,d   Grzechnik, Anna a,c   Grzechnik, Slawomir K a,e   Han, Gye Won a,c   more..


Author keywords

crystal structure; DNA repair; Mre11; nuclease; structural genomics

Indexed keywords

DNA; DOUBLE STRANDED DNA; HISTIDINE; MRE11 PROTEIN; SINGLE STRANDED DNA;

EID: 77649338640     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.049     Document Type: Article
Times cited : (38)

References (69)
  • 1
    • 0024195429 scopus 로고
    • DNA damage produced by ionizing radiation in mammalian cells: identities, mechanisms of formation, and reparability
    • Ward J.F. DNA damage produced by ionizing radiation in mammalian cells: identities, mechanisms of formation, and reparability. Prog. Nucleic Acid Res. Mol. Biol. 35 (1988) 95-125
    • (1988) Prog. Nucleic Acid Res. Mol. Biol. , vol.35 , pp. 95-125
    • Ward, J.F.1
  • 2
    • 0030946855 scopus 로고    scopus 로고
    • Deletions at stalled replication forks occur by two different pathways
    • Bierne H., Ehrlich S.D., and Michel B. Deletions at stalled replication forks occur by two different pathways. EMBO J. 16 (1997) 3332-3340
    • (1997) EMBO J. , vol.16 , pp. 3332-3340
    • Bierne, H.1    Ehrlich, S.D.2    Michel, B.3
  • 3
    • 0030966099 scopus 로고    scopus 로고
    • Recent advances in understanding V(D)J recombination
    • Gellert M. Recent advances in understanding V(D)J recombination. Adv. Immunol. 64 (1997) 39-64
    • (1997) Adv. Immunol. , vol.64 , pp. 39-64
    • Gellert, M.1
  • 4
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • Michel B., Ehrlich S.D., and Uzest M. DNA double-strand breaks caused by replication arrest. EMBO J. 16 (1997) 430-438
    • (1997) EMBO J. , vol.16 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 5
    • 34948899943 scopus 로고    scopus 로고
    • Mre11-Rad50-Nbs1 is a keystone complex connecting DNA repair machinery, double-strand break signaling, and the chromatin template
    • Williams R.S., Williams J.S., and Tainer J.A. Mre11-Rad50-Nbs1 is a keystone complex connecting DNA repair machinery, double-strand break signaling, and the chromatin template. Biochem. Cell Biol. 85 (2007) 509-520
    • (2007) Biochem. Cell Biol. , vol.85 , pp. 509-520
    • Williams, R.S.1    Williams, J.S.2    Tainer, J.A.3
  • 7
    • 0030089480 scopus 로고    scopus 로고
    • The sbcC and sbcD genes of Escherichia coli encode a nuclease involved in palindrome inviability and genetic recombination
    • Connelly J.C., and Leach D.R. The sbcC and sbcD genes of Escherichia coli encode a nuclease involved in palindrome inviability and genetic recombination. Genes Cells 1 (1996) 285-291
    • (1996) Genes Cells , vol.1 , pp. 285-291
    • Connelly, J.C.1    Leach, D.R.2
  • 8
    • 0032085295 scopus 로고    scopus 로고
    • The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks
    • Paull T.T., and Gellert M. The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell 1 (1998) 969-979
    • (1998) Mol. Cell , vol.1 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 9
    • 0035930342 scopus 로고    scopus 로고
    • Promotion of Dnl4-catalyzed DNA end-joining by the Rad50/Mre11/Xrs2 and Hdf1/Hdf2 complexes
    • Chen L., Trujillo K., Ramos W., Sung P., and Tomkinson A.E. Promotion of Dnl4-catalyzed DNA end-joining by the Rad50/Mre11/Xrs2 and Hdf1/Hdf2 complexes. Mol. Cell 8 (2001) 1105-1115
    • (2001) Mol. Cell , vol.8 , pp. 1105-1115
    • Chen, L.1    Trujillo, K.2    Ramos, W.3    Sung, P.4    Tomkinson, A.E.5
  • 10
    • 0036682830 scopus 로고    scopus 로고
    • Tethering on the brink: the evolutionarily conserved Mre11-Rad50 complex
    • Connelly J.C., and Leach D.R. Tethering on the brink: the evolutionarily conserved Mre11-Rad50 complex. Trends Biochem. Sci. 27 (2002) 410-418
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 410-418
    • Connelly, J.C.1    Leach, D.R.2
  • 12
    • 0035906860 scopus 로고    scopus 로고
    • Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase
    • Hopfner K.P., Karcher A., Craig L., Woo T.T., Carney J.P., and Tainer J.A. Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Cell 105 (2001) 473-485
    • (2001) Cell , vol.105 , pp. 473-485
    • Hopfner, K.P.1    Karcher, A.2    Craig, L.3    Woo, T.T.4    Carney, J.P.5    Tainer, J.A.6
  • 13
    • 0035695023 scopus 로고    scopus 로고
    • Recombination at double-strand breaks and DNA ends: conserved mechanisms from phage to humans
    • Cromie G.A., Connelly J.C., and Leach D.R. Recombination at double-strand breaks and DNA ends: conserved mechanisms from phage to humans. Mol. Cell 8 (2001) 1163-1174
    • (2001) Mol. Cell , vol.8 , pp. 1163-1174
    • Cromie, G.A.1    Connelly, J.C.2    Leach, D.R.3
  • 14
    • 0036276388 scopus 로고    scopus 로고
    • The Mre11 complex: at the crossroads of dna repair and checkpoint signalling
    • D'Amours D., and Jackson S.P. The Mre11 complex: at the crossroads of dna repair and checkpoint signalling. Nat. Rev. Mol. Cell Biol. 3 (2002) 317-327
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 317-327
    • D'Amours, D.1    Jackson, S.P.2
  • 15
    • 19344370467 scopus 로고    scopus 로고
    • Mechanism of DNA double-strand break repair by non-homologous end joining
    • Hefferin M.L., and Tomkinson A.E. Mechanism of DNA double-strand break repair by non-homologous end joining. DNA Repair 4 (2005) 639-648
    • (2005) DNA Repair , vol.4 , pp. 639-648
    • Hefferin, M.L.1    Tomkinson, A.E.2
  • 16
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae
    • Paques F., and Haber J.E. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63 (1999) 349-404
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 349-404
    • Paques, F.1    Haber, J.E.2
  • 17
    • 34347379540 scopus 로고    scopus 로고
    • Additive effects of SbcCD and PolX deficiencies in the in vivo repair of DNA double-strand breaks in Deinococcus radiodurans
    • Bentchikou E., Servant P., Coste G., and Sommer S. Additive effects of SbcCD and PolX deficiencies in the in vivo repair of DNA double-strand breaks in Deinococcus radiodurans. J. Bacteriol. 189 (2007) 4784-4790
    • (2007) J. Bacteriol. , vol.189 , pp. 4784-4790
    • Bentchikou, E.1    Servant, P.2    Coste, G.3    Sommer, S.4
  • 18
    • 0028857690 scopus 로고
    • Structural and functional similarities between the SbcCD proteins of Escherichia coli and the RAD50 and MRE11 (RAD32) recombination and repair proteins of yeast
    • Sharples G.J., and Leach D.R. Structural and functional similarities between the SbcCD proteins of Escherichia coli and the RAD50 and MRE11 (RAD32) recombination and repair proteins of yeast. Mol. Microbiol. 17 (1995) 1215-1217
    • (1995) Mol. Microbiol. , vol.17 , pp. 1215-1217
    • Sharples, G.J.1    Leach, D.R.2
  • 19
    • 0000770165 scopus 로고    scopus 로고
    • Nijmegen breakage syndrome. The International Nijmegen Breakage Syndrome Study Group
    • Nijmegen breakage syndrome. The International Nijmegen Breakage Syndrome Study Group. Arch. Dis. Child. 82 (2000) 400-406
    • (2000) Arch. Dis. Child. , vol.82 , pp. 400-406
  • 20
    • 0008158443 scopus 로고
    • Radiosensitivity in ataxia-telangiectasia: a new explanation
    • Painter R.B., and Young B.R. Radiosensitivity in ataxia-telangiectasia: a new explanation. Proc. Natl Acad. Sci. USA 77 (1980) 7315-7317
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7315-7317
    • Painter, R.B.1    Young, B.R.2
  • 21
    • 0033544724 scopus 로고    scopus 로고
    • The DNA double-strand break repair gene hMRE11 is mutated in individuals with an ataxia-telangiectasia-like disorder
    • Stewart G.S., Maser R.S., Stankovic T., Bressan D.A., Kaplan M.I., Jaspers N.G., et al. The DNA double-strand break repair gene hMRE11 is mutated in individuals with an ataxia-telangiectasia-like disorder. Cell 99 (1999) 577-587
    • (1999) Cell , vol.99 , pp. 577-587
    • Stewart, G.S.1    Maser, R.S.2    Stankovic, T.3    Bressan, D.A.4    Kaplan, M.I.5    Jaspers, N.G.6
  • 22
    • 0041689960 scopus 로고    scopus 로고
    • The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint
    • Chahwan C., Nakamura T.M., Sivakumar S., Russell P., and Rhind N. The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint. Mol. Cell. Biol. 23 (2003) 6564-6573
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6564-6573
    • Chahwan, C.1    Nakamura, T.M.2    Sivakumar, S.3    Russell, P.4    Rhind, N.5
  • 23
    • 56649086648 scopus 로고    scopus 로고
    • Aberrations of the MRE11-RAD50-NBS1 DNA damage sensor complex in human breast cancer: MRE11 as a candidate familial cancer-predisposing gene
    • Bartkova J., Tommiska J., Oplustilova L., Aaltonen K., Tamminen A., Heikkinen T., et al. Aberrations of the MRE11-RAD50-NBS1 DNA damage sensor complex in human breast cancer: MRE11 as a candidate familial cancer-predisposing gene. Mol. Oncol. 2 (2008) 296-316
    • (2008) Mol. Oncol. , vol.2 , pp. 296-316
    • Bartkova, J.1    Tommiska, J.2    Oplustilova, L.3    Aaltonen, K.4    Tamminen, A.5    Heikkinen, T.6
  • 25
    • 0035692142 scopus 로고    scopus 로고
    • Overlapping functions of the Saccharomyces cerevisiae Mre11, Exo1 and Rad27 nucleases in DNA metabolism
    • Moreau S., Morgan E.A., and Symington L.S. Overlapping functions of the Saccharomyces cerevisiae Mre11, Exo1 and Rad27 nucleases in DNA metabolism. Genetics 159 (2001) 1423-1433
    • (2001) Genetics , vol.159 , pp. 1423-1433
    • Moreau, S.1    Morgan, E.A.2    Symington, L.S.3
  • 27
    • 52949149420 scopus 로고    scopus 로고
    • Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair
    • Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., et al. Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair. Cell 135 (2008) 97-109
    • (2008) Cell , vol.135 , pp. 97-109
    • Williams, R.S.1    Moncalian, G.2    Williams, J.S.3    Yamada, Y.4    Limbo, O.5    Shin, D.S.6
  • 30
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • Aravind L., and Koonin E.V. Phosphoesterase domains associated with DNA polymerases of diverse origins. Nucleic Acids Res. 26 (1998) 3746-3752
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 31
    • 0032493294 scopus 로고    scopus 로고
    • The SbcCD nuclease of Escherichia coli is a structural maintenance of chromosomes (SMC) family protein that cleaves hairpin DNA
    • Connelly J.C., Kirkham L.A., and Leach D.R. The SbcCD nuclease of Escherichia coli is a structural maintenance of chromosomes (SMC) family protein that cleaves hairpin DNA. Proc. Natl Acad. Sci. USA 95 (1998) 7969-7974
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7969-7974
    • Connelly, J.C.1    Kirkham, L.A.2    Leach, D.R.3
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computing Project Number 4
    • Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 34
    • 0032031476 scopus 로고    scopus 로고
    • Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of gammaB- and betaB2-crystallin
    • Tickle I.J., Laskowski R.A., and Moss D.S. Error estimates of protein structure coordinates and deviations from standard geometry by full-matrix refinement of gammaB- and betaB2-crystallin. Acta Crystallogr. D 54 (1998) 243-252
    • (1998) Acta Crystallogr. D , vol.54 , pp. 243-252
    • Tickle, I.J.1    Laskowski, R.A.2    Moss, D.S.3
  • 35
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 36
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis I.W., Murray L.W., Richardson J.S., and Richardson D.C. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32 (2004) W615-W619
    • (2004) Nucleic Acids Res. , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 37
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • Mol C.D., Izumi T., Mitra S., and Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature 403 (2000) 451-456
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 38
    • 0029133116 scopus 로고
    • X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex
    • Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A., Fitzgibbon M.J., et al. X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell 82 (1995) 507-522
    • (1995) Cell , vol.82 , pp. 507-522
    • Griffith, J.P.1    Kim, J.L.2    Kim, E.E.3    Sintchak, M.D.4    Thomson, J.A.5    Fitzgibbon, M.J.6
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0032127358 scopus 로고    scopus 로고
    • The Biology Workbench - a seamless database and analysis environment for the biologist. Proteins:
    • Subramaniam S. The Biology Workbench - a seamless database and analysis environment for the biologist. Proteins:. Struct. Funct. Genet. 32 (1998) 1-2
    • (1998) Struct. Funct. Genet. , vol.32 , pp. 1-2
    • Subramaniam, S.1
  • 41
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., and Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11 (1998) 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 42
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 43
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 44
    • 0031664401 scopus 로고    scopus 로고
    • Alteration of N-terminal phosphoesterase signature motifs inactivates Saccharomyces cerevisiae Mre11
    • Bressan D.A., Olivares H.A., Nelms B.E., and Petrini J.H. Alteration of N-terminal phosphoesterase signature motifs inactivates Saccharomyces cerevisiae Mre11. Genetics 150 (1998) 591-600
    • (1998) Genetics , vol.150 , pp. 591-600
    • Bressan, D.A.1    Olivares, H.A.2    Nelms, B.E.3    Petrini, J.H.4
  • 45
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 48
    • 20144386860 scopus 로고    scopus 로고
    • Structural insights into the first incision reaction during nucleotide excision repair
    • Truglio J.J., Rhau B., Croteau D.L., Wang L., Skorvaga M., Karakas E., et al. Structural insights into the first incision reaction during nucleotide excision repair. EMBO J. 24 (2005) 885-894
    • (2005) EMBO J. , vol.24 , pp. 885-894
    • Truglio, J.J.1    Rhau, B.2    Croteau, D.L.3    Wang, L.4    Skorvaga, M.5    Karakas, E.6
  • 50
    • 0037398027 scopus 로고    scopus 로고
    • Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures
    • Hopfner K.P., and Tainer J.A. Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures. Curr. Opin. Struct. Biol. 13 (2003) 249-255
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 249-255
    • Hopfner, K.P.1    Tainer, J.A.2
  • 51
    • 0037015054 scopus 로고    scopus 로고
    • Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
    • Lesley S.A., Kuhn P., Godzik A., Deacon A.M., Mathews I., Kreusch A., et al. Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline. Proc. Natl Acad. Sci. USA 99 (2002) 11664-11669
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11664-11669
    • Lesley, S.A.1    Kuhn, P.2    Godzik, A.3    Deacon, A.M.4    Mathews, I.5    Kreusch, A.6
  • 52
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins
    • Klock H.E., Koesema E.J., Knuth M.W., and Lesley S.A. Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins. Struct. Funct. Genet. 71 (2008) 982-994
    • (2008) Struct. Funct. Genet. , vol.71 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 54
    • 0036896410 scopus 로고    scopus 로고
    • An automated system to mount cryo-cooled protein crystals on a synchrotron beamline, using compact sample cassettes and a small-scale robot
    • Cohen A.E., Ellis P.J., Miller M.D., Deacon A.M., and Phizackerley R.P. An automated system to mount cryo-cooled protein crystals on a synchrotron beamline, using compact sample cassettes and a small-scale robot. J. Appl. Crystallogr. 2002 (2002) 720-726
    • (2002) J. Appl. Crystallogr. , vol.2002 , pp. 720-726
    • Cohen, A.E.1    Ellis, P.J.2    Miller, M.D.3    Deacon, A.M.4    Phizackerley, R.P.5
  • 55
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips T.M., McPhillips S.E., Chiu H.J., Cohen A.E., Deacon A.M., Ellis P.J., et al. Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines. J. Synchrotron Radiat. 9 (2002) 401-406
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 401-406
    • McPhillips, T.M.1    McPhillips, S.E.2    Chiu, H.J.3    Cohen, A.E.4    Deacon, A.M.5    Ellis, P.J.6
  • 56
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 59
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 60
    • 0038793604 scopus 로고    scopus 로고
    • Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement
    • Terwilliger T.C. Improving macromolecular atomic models at moderate resolution by automated iterative model building, statistical density modification and refinement. Acta Crystallogr. D 59 (2003) 1174-1182
    • (2003) Acta Crystallogr. D , vol.59 , pp. 1174-1182
    • Terwilliger, T.C.1
  • 61
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie, A. G. W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newsletter Protein Crystallogr. No. 26.
    • (1992) Joint CCP4+ESF-EAMCB Newsletter Protein Crystallogr , Issue.26
    • Leslie, A.G.W.1
  • 62
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 63
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn M.D., Murshudov G.N., and Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374 (2003) 300-321
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 64
    • 16644393507 scopus 로고    scopus 로고
    • Automated and accurate deposition of structures solved by X-ray diffraction to the Protein Data Bank
    • Yang H., Guranovic V., Dutta S., Feng Z., Berman H.M., and Westbrook J.D. Automated and accurate deposition of structures solved by X-ray diffraction to the Protein Data Bank. Acta Crystallogr. D 60 (2004) 1833-1839
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1833-1839
    • Yang, H.1    Guranovic, V.2    Dutta, S.3    Feng, Z.4    Berman, H.M.5    Westbrook, J.D.6
  • 65
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8 (1990) 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 66
    • 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., and Wodak S.J. 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 (1999) 191-205
    • (1999) Acta Crystallogr. D , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 67
    • 0034013435 scopus 로고    scopus 로고
    • Validation of protein crystal structures
    • Kleywegt G.J. Validation of protein crystal structures. Acta Crystallogr. D 56 (2000) 249-265
    • (2000) Acta Crystallogr. D , vol.56 , pp. 249-265
    • Kleywegt, G.J.1
  • 68
    • 13444254300 scopus 로고    scopus 로고
    • PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids
    • Laskowski R.A., Chistyakov V.V., and Thornton J.M. PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids. Nucleic Acids Res. 33 (2005) D266-D268
    • (2005) Nucleic Acids Res. , vol.33
    • Laskowski, R.A.1    Chistyakov, V.V.2    Thornton, J.M.3
  • 69
    • 0842302302 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System, Palo Alto, CA, USA www.pymol.org
    • DeLano W.L. DeLano Scientific LLC (2002), The PyMOL Molecular Graphics System, Palo Alto, CA, USA. http://www.pymol.org www.pymol.org
    • (2002) DeLano Scientific LLC
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.