메뉴 건너뛰기




Volumn 496, Issue 7446, 2013, Pages 477-481

Accurate assessment of mass, models and resolution by small-angle scattering

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY ASSESSMENT; ANALYTICAL FRAMEWORK; DATA ACQUISITION; EXPERIMENTAL STUDY; IMAGE RESOLUTION; NUMERICAL MODEL; PROTEIN; RNA; SCATTERING; STATISTICAL ANALYSIS; THERMODYNAMICS;

EID: 84876800465     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12070     Document Type: Article
Times cited : (621)

References (32)
  • 1
    • 35748938227 scopus 로고    scopus 로고
    • Comments on the NIGMS PSI
    • Harrison, S. C. Comments on the NIGMS PSI. Structure 15, 1344-1346 (2007).
    • (2007) Structure , vol.15 , pp. 1344-1346
    • Harrison, S.C.1
  • 2
    • 68349097394 scopus 로고    scopus 로고
    • Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
    • Hura, G. L. et al. Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS). Nature Methods 6, 606-612 (2009).
    • (2009) Nature Methods , vol.6 , pp. 606-612
    • Hura, G.L.1
  • 3
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: Comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • Rambo, R. P. & Tainer, J. A. Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering. Curr. Opin. Struct. Biol. 20, 128-137 (2010).
    • (2010) Curr. Opin. Struct. Biol , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 4
    • 79958049200 scopus 로고    scopus 로고
    • New era ofmolecular structure and dynamics from solution scattering experiments
    • Sosnick, T. R. &Woodson, S. A. New era ofmolecular structure and dynamics from solution scattering experiments. Biopolymers 95, 503-504 (2011).
    • (2011) Biopolymers , vol.95 , pp. 503-504
    • Sosnick, T.R.1    Woodson, S.A.2
  • 6
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam, C. D., Hammel, M., Hura, G. L. & Tainer, J. A. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40, 191-285 (2007).
    • (2007) Q. Rev. Biophys , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 7
    • 77950223101 scopus 로고    scopus 로고
    • Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls
    • Jacques, D. A. & Trewhella, J. Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls. Protein Sci. 19, 642-657 (2010).
    • (2010) Protein Sci , vol.19 , pp. 642-657
    • Jacques, D.A.1    Trewhella, J.2
  • 8
    • 12844260994 scopus 로고    scopus 로고
    • Probing counterion modulated repulsion and attraction between nucleic acid duplexes in solution
    • Bai, Y., Das, R., Millett, I. S., Herschlag, D. & Doniach, S. Probing counterion modulated repulsion and attraction between nucleic acid duplexes in solution. Proc. Natl Acad. Sci. USA 102, 1035-1040 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1035-1040
    • Bai, Y.1    Das, R.2    Millett, I.S.3    Herschlag, D.4    Doniach, S.5
  • 9
    • 0000403125 scopus 로고
    • Small-angle scattering. Information content and error analysis
    • Moore, P. Small-angle scattering. Information content and error analysis. J. Appl. Crystallogr. 13, 168-175 (1980).
    • (1980) J. Appl. Crystallogr , vol.13 , pp. 168-175
    • Moore, P.1
  • 10
    • 77149170364 scopus 로고    scopus 로고
    • Improving small-angle X-ray scattering data for structural analyses of the RNA world
    • Rambo, R. P. & Tainer, J. A. Improving small-angle X-ray scattering data for structural analyses of the RNA world. RNA 16, 638-646 (2010).
    • (2010) RNA , vol.16 , pp. 638-646
    • Rambo, R.P.1    Tainer, J.A.2
  • 11
    • 71449098436 scopus 로고    scopus 로고
    • Structural mechanism of abscisic acid binding and signaling by dimeric PYR1
    • Nishimura, N. et al. Structural mechanism of abscisic acid binding and signaling by dimeric PYR1. Science 326, 1373-1379 (2009).
    • (2009) Science , vol.326 , pp. 1373-1379
    • Nishimura, N.1
  • 12
    • 71549134755 scopus 로고    scopus 로고
    • Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs
    • Santiago, J. et al. Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs. Plant J. 60, 575-588 (2009).
    • (2009) Plant J , vol.60 , pp. 575-588
    • Santiago, J.1
  • 13
    • 77954627025 scopus 로고    scopus 로고
    • Free state conformational sampling of the SAM-I riboswitch aptamer domain
    • Stoddard, C. D. et al. Free state conformational sampling of the SAM-I riboswitch aptamer domain. Structure 18, 787-797 (2010).
    • (2010) Structure , vol.18 , pp. 787-797
    • Stoddard, C.D.1
  • 14
    • 77954758121 scopus 로고    scopus 로고
    • Multi-domain packing in the aminoacylatable 39 end of a plant viral RNA
    • Hammond, J. A., Rambo, R. P. & Kieft, J. S. Multi-domain packing in the aminoacylatable 39 end of a plant viral RNA. J. Mol. Biol. 399, 450-463 (2010).
    • (2010) J. Mol. Biol , vol.399 , pp. 450-463
    • Hammond, J.A.1    Rambo, R.P.2    Kieft, J.S.3
  • 15
    • 0034484513 scopus 로고    scopus 로고
    • SAXS experiments on absolute scale with Kratky systems using water as a secondary standard
    • Orthaber, D., Bergmann, A. & Glatter, O. SAXS experiments on absolute scale with Kratky systems using water as a secondary standard. J. Appl. Crystallogr. 33, 218-225 (2000).
    • (2000) J. Appl. Crystallogr , vol.33 , pp. 218-225
    • Orthaber, D.1    Bergmann, A.2    Glatter, O.3
  • 16
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy ofmolecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas, E. & Svergun, D. I. Accuracy ofmolecular mass determination of proteins in solution by small-angle X-ray scattering. J. Appl. Crystallogr. 40, s245-s249 (2007).
    • (2007) J. Appl. Crystallogr , vol.40
    • Mylonas, E.1    Svergun, D.I.2
  • 17
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single smallangle X-ray scattering measurement on a relative scale
    • Fischer, H., de Oliveira Neto, M., Napolitano, H. B., Polikarpov, I. & Craievich, A. F. Determination of the molecular weight of proteins in solution from a single smallangle X-ray scattering measurement on a relative scale. J. Appl. Crystallogr. 43, 101-109 (2010).
    • (2010) J. Appl. Crystallogr , vol.43 , pp. 101-109
    • Fischer, H.1    De Oliveira Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 18
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo, R. P. & Tainer, J. A. Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law. Biopolymers 95, 559-571 (2011).
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 19
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H. M. et al.The Protein DataBank.Nucleic Acids Res.28, 235-242(2000).
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 20
    • 0027498262 scopus 로고
    • Light scattering and the absolute characterization of macromolecules
    • Wyatt, P. J. Light scattering and the absolute characterization of macromolecules. Anal. Chim. Acta 272, 1-40 (1993).
    • (1993) Anal. Chim. Acta , vol.272 , pp. 1-40
    • Wyatt, P.J.1
  • 21
    • 0029185933 scopus 로고
    • CRYSOL-A program to evaluate X-ray solution scattering of biologicalmacromolecules fromatomic coordinates
    • Svergun, D., Barberato, C. & Koch, M. H. J. CRYSOL-a program to evaluate X-ray solution scattering of biologicalmacromolecules fromatomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995).
    • (1995) J. Appl. Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 22
    • 77954280480 scopus 로고    scopus 로고
    • A web server for rapid computation and fitting of SAXS profiles
    • Schneidman-Duhovny, D., Hammel, M. & Sali, A. FoXS: a web server for rapid computation and fitting of SAXS profiles. Nucleic Acids Res. 38, W540-W544 (2010).
    • (2010) Nucleic Acids Res , vol.38
    • Schneidman-Duhovny, D.1    Hammel, M.2    Foxs, S.A.3
  • 23
    • 0026597444 scopus 로고
    • FreeR value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Bruger, A. T. FreeR value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
    • (1992) Nature , vol.355 , pp. 472-475
    • Bruger, A.T.1
  • 24
    • 0027918891 scopus 로고
    • Assessing the quality of solution nuclear magnetic resonance structures by complete crossvalidation
    • Bruger, A. T., Clore, G. M., Gronenborn, A. M., Saffrich, R.&Nilges, M. Assessing the quality of solution nuclear magnetic resonance structures by complete crossvalidation. Science 261, 328-331 (1993).
    • (1993) Science , vol.261 , pp. 328-331
    • Bruger, A.T.1    Clore, G.M.2    Gronenborn, A.M.3    Saffrich, R.4    Nilges, M.5
  • 27
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A. & Diederichs, K. Linking crystallographic model and data quality. Science 336, 1030-1033 (2012).
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 28
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Bruger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr , vol.D 54 , pp. 905-921
    • Bruger, A.T.1
  • 29
    • 0030931612 scopus 로고    scopus 로고
    • Prediction of protein conformational freedom from distance constraints
    • de Groot, B. L. et al. Prediction of protein conformational freedom from distance constraints. Proteins 29, 240-251 (1997).
    • (1997) Proteins , vol.29 , pp. 240-251
    • De Groot, B.L.1
  • 30
    • 2542540696 scopus 로고    scopus 로고
    • Assembly of an active group II intron-maturase complex by protein dimerization
    • Rambo, R. P. & Doudna, J. A. Assembly of an active group II intron-maturase complex by protein dimerization. Biochemistry 43, 6486-6497 (2004).
    • (2004) Biochemistry , vol.43 , pp. 6486-6497
    • Rambo, R.P.1    Doudna, J.A.2
  • 31
    • 84055212199 scopus 로고    scopus 로고
    • Structural architecture of an RNA that competitively inhibits RNase L
    • Keel, A. Y., Jha, B. K. & Kieft, J. S. Structural architecture of an RNA that competitively inhibits RNase L. RNA 18, 88-89 (2012).
    • (2012) RNA , vol.18 , pp. 88-89
    • Keel, A.Y.1    Jha, B.K.2    Kieft, J.S.3
  • 32
    • 44849090619 scopus 로고    scopus 로고
    • Analyzing the flexibility of RNA structures by constraint counting
    • Fulle, S. & Gohlke, H. Analyzing the flexibility of RNA structures by constraint counting. Biophys. J. 94, 4202-4219 (2008).
    • (2008) Biophys. J , vol.94 , pp. 4202-4219
    • Fulle, S.1    Gohlke, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.