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Volumn 24, Issue 4, 2013, Pages 716-723

Modern X-ray scattering studies of complex biological systems

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX BIOLOGICAL SYSTEMS; INTERACTION STUDIES; LOWER RESOLUTION; MONODISPERSITY; STRUCTURAL CHARACTERIZATION; SURROUNDING ENVIRONMENT;

EID: 84880938796     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2013.01.005     Document Type: Review
Times cited : (23)

References (87)
  • 1
    • 72449208673 scopus 로고    scopus 로고
    • Gel-expanded to gel-condensed transition in neurofilament networks revealed by direct force measurements
    • Beck R., Deek J., Jones J.B., Safinya C.R. Gel-expanded to gel-condensed transition in neurofilament networks revealed by direct force measurements. Nat Mater 2010, 9:40-46.
    • (2010) Nat Mater , vol.9 , pp. 40-46
    • Beck, R.1    Deek, J.2    Jones, J.B.3    Safinya, C.R.4
  • 4
    • 84863643938 scopus 로고    scopus 로고
    • Automated acquisition and analysis of small angle X-ray scattering data
    • Franke D., Kikhney A.G., Svergun D.I. Automated acquisition and analysis of small angle X-ray scattering data. Nucl Instrum Methods A 2012, 689:52-59.
    • (2012) Nucl Instrum Methods A , vol.689 , pp. 52-59
    • Franke, D.1    Kikhney, A.G.2    Svergun, D.I.3
  • 5
    • 84859744221 scopus 로고    scopus 로고
    • Nika: software for two-dimensional data reduction
    • Ilavsky J. Nika: software for two-dimensional data reduction. J Appl Crystallogr 2012, 45:324-328.
    • (2012) J Appl Crystallogr , vol.45 , pp. 324-328
    • Ilavsky, J.1
  • 7
    • 62649168361 scopus 로고    scopus 로고
    • Irena: tool suite for modeling and analysis of small-angle scattering
    • Ilavsky J., Jemian P.R. Irena: tool suite for modeling and analysis of small-angle scattering. J Appl Crystallogr 2009, 42:347-353.
    • (2009) J Appl Crystallogr , vol.42 , pp. 347-353
    • Ilavsky, J.1    Jemian, P.R.2
  • 8
    • 78649503199 scopus 로고    scopus 로고
    • X plus: a comprehensive computationally accelerated structure analysis tool for solution X-ray scattering from supramolecular self-assemblies
    • Ben-Nun T., Ginsburg A., Szekely P., Raviv U. X plus: a comprehensive computationally accelerated structure analysis tool for solution X-ray scattering from supramolecular self-assemblies. J Appl Crystallogr 2010, 43:1522-1531.
    • (2010) J Appl Crystallogr , vol.43 , pp. 1522-1531
    • Ben-Nun, T.1    Ginsburg, A.2    Szekely, P.3    Raviv, U.4
  • 10
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke D., Svergun D.I. DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J Appl Crystallogr 2009, 42:342-346.
    • (2009) J Appl Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 11
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., Koch M.H.J. Determination of domain structure of proteins from X-ray solution scattering. Biophys J 2001, 80:2946-2953.
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 12
    • 34248363563 scopus 로고    scopus 로고
    • Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography
    • Tsutakawa S.E., Hura G.L., Frankel K.A., Cooper P.K., Tainer J.A. Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography. J Struct Biol 2007, 158:214-223.
    • (2007) J Struct Biol , vol.158 , pp. 214-223
    • Tsutakawa, S.E.1    Hura, G.L.2    Frankel, K.A.3    Cooper, P.K.4    Tainer, J.A.5
  • 13
    • 34249894142 scopus 로고    scopus 로고
    • Small-angle X-ray scattering from RNA, proteins, and protein complexes
    • Lipfert J., Doniach S. Small-angle X-ray scattering from RNA, proteins, and protein complexes. Annu Rev Biophys Biomol Struct 2007, 36:307-327.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 307-327
    • Lipfert, J.1    Doniach, S.2
  • 14
    • 77951296391 scopus 로고    scopus 로고
    • Characterization of proteins with wide-angle X-ray solution scattering (WAXS)
    • Makowski L. Characterization of proteins with wide-angle X-ray solution scattering (WAXS). J Struct Funct Genomics 2010, 11:9-19.
    • (2010) J Struct Funct Genomics , vol.11 , pp. 9-19
    • Makowski, L.1
  • 15
    • 84865525834 scopus 로고    scopus 로고
    • Integrative structural modeling with small angle X-ray scattering profiles
    • Schneidman-Duhovny D., Kim S.J., Sali A. Integrative structural modeling with small angle X-ray scattering profiles. BMC Struct Biol 2012, 12.
    • (2012) BMC Struct Biol , pp. 12
    • Schneidman-Duhovny, D.1    Kim, S.J.2    Sali, A.3
  • 16
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernado P., Mylonas E., Petoukhov M.V., Blackledge M., Svergun D.I. Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc 2007, 129:5656-5664.
    • (2007) J Am Chem Soc , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 17
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • Pelikan M., Hura G.L., Hammel M. Structure and flexibility within proteins as identified through small angle X-ray scattering. Gen Physiol Biophys 2009, 28:174-189.
    • (2009) Gen Physiol Biophys , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 18
    • 78650948314 scopus 로고    scopus 로고
    • SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions
    • Rozycki B., Kim Y.C., Hummer G. SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions. Structure 2011, 19:109-116.
    • (2011) Structure , vol.19 , pp. 109-116
    • Rozycki, B.1    Kim, Y.C.2    Hummer, G.3
  • 19
    • 79958037883 scopus 로고    scopus 로고
    • Constructing ensembles for intrinsically disordered proteins
    • Fisher C.K., Stultz C.M. Constructing ensembles for intrinsically disordered proteins. Curr Opin Struct Biol 2011, 21:426-431.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 426-431
    • Fisher, C.K.1    Stultz, C.M.2
  • 20
    • 68949116065 scopus 로고    scopus 로고
    • A rapid coarse residue-based computational method for X-ray solution scattering characterization of protein folds and multiple conformational states of large protein complexes
    • Yang S.C., Park S., Makowski L., Roux B. A rapid coarse residue-based computational method for X-ray solution scattering characterization of protein folds and multiple conformational states of large protein complexes. Biophys J 2009, 96:4449-4463.
    • (2009) Biophys J , vol.96 , pp. 4449-4463
    • Yang, S.C.1    Park, S.2    Makowski, L.3    Roux, B.4
  • 21
    • 67649373298 scopus 로고    scopus 로고
    • Intrinsic dynamics of restriction endonuclease EcoO109I studied by molecular dynamics simulations and X-ray scattering data analysis
    • Oroguchi T., Hashimoto H., Shimizu T., Sato M., Ikeguchi M. Intrinsic dynamics of restriction endonuclease EcoO109I studied by molecular dynamics simulations and X-ray scattering data analysis. Biophys J 2009, 96:2808-2822.
    • (2009) Biophys J , vol.96 , pp. 2808-2822
    • Oroguchi, T.1    Hashimoto, H.2    Shimizu, T.3    Sato, M.4    Ikeguchi, M.5
  • 23
    • 79955846859 scopus 로고    scopus 로고
    • SAXS studies of ion-nucleic acid interactions
    • Pollack L. SAXS studies of ion-nucleic acid interactions. Annu Rev Biophys 2011, 40:225-242.
    • (2011) Annu Rev Biophys , vol.40 , pp. 225-242
    • Pollack, L.1
  • 24
    • 40849086267 scopus 로고    scopus 로고
    • Simultaneous estimation of the form factor and structure factor for globular particles in small-angle scattering
    • Hansen S. Simultaneous estimation of the form factor and structure factor for globular particles in small-angle scattering. J Appl Crystallogr 2008, 41:436-445.
    • (2008) J Appl Crystallogr , vol.41 , pp. 436-445
    • Hansen, S.1
  • 25
    • 0020905807 scopus 로고
    • Determination of micelle structure and charge by neutron small-angle scattering
    • Hayter J.B., Penfold J. Determination of micelle structure and charge by neutron small-angle scattering. Colloid Polym Sci 1983, 261:1022-1030.
    • (1983) Colloid Polym Sci , vol.261 , pp. 1022-1030
    • Hayter, J.B.1    Penfold, J.2
  • 27
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • Svergun D.I., Koch M.H.J. Small-angle scattering studies of biological macromolecules in solution. Rep Prog Phys 2003, 66:1735-1782.
    • (2003) Rep Prog Phys , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 28
    • 84864478612 scopus 로고    scopus 로고
    • High concentration formulation studies of an IgG2 antibody using small angle X-ray scattering
    • Mosbaek C.R., Konarev P.V., Svergun D.I., Rischel C., Vestergaard B. High concentration formulation studies of an IgG2 antibody using small angle X-ray scattering. Pharmaceut Res 2012, 29:2225-2235.
    • (2012) Pharmaceut Res , vol.29 , pp. 2225-2235
    • Mosbaek, C.R.1    Konarev, P.V.2    Svergun, D.I.3    Rischel, C.4    Vestergaard, B.5
  • 30
    • 0032484699 scopus 로고    scopus 로고
    • Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes
    • Curtis R.A., Prausnitz J.M., Blanch H.W. Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnol Bioeng 1998, 57:11-21.
    • (1998) Biotechnol Bioeng , vol.57 , pp. 11-21
    • Curtis, R.A.1    Prausnitz, J.M.2    Blanch, H.W.3
  • 31
    • 84855921181 scopus 로고    scopus 로고
    • Theoretical description of cluster formation in two-Yukawa competing fluids
    • Costa D., Caccamo C., Bomont J.M., Bretonnet J.L. Theoretical description of cluster formation in two-Yukawa competing fluids. Mol Phys 2011, 109:2845-2853.
    • (2011) Mol Phys , vol.109 , pp. 2845-2853
    • Costa, D.1    Caccamo, C.2    Bomont, J.M.3    Bretonnet, J.L.4
  • 32
    • 0037215795 scopus 로고    scopus 로고
    • Protein interactions in undersaturated and supersaturated solutions: a study using light and X-ray scattering
    • Narayanan J., Liu X.Y. Protein interactions in undersaturated and supersaturated solutions: a study using light and X-ray scattering. Biophys J 2003, 84:523-532.
    • (2003) Biophys J , vol.84 , pp. 523-532
    • Narayanan, J.1    Liu, X.Y.2
  • 33
    • 77949805991 scopus 로고    scopus 로고
    • Protein-protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations
    • Ianeselli L., Zhang F.J., Skoda M.W.A., Jacobs R.M.J., Martin R.A., Callow S., Prevost S., Schreiber F. Protein-protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations. J Phys Chem B 2010, 114:3776-3783.
    • (2010) J Phys Chem B , vol.114 , pp. 3776-3783
    • Ianeselli, L.1    Zhang, F.J.2    Skoda, M.W.A.3    Jacobs, R.M.J.4    Martin, R.A.5    Callow, S.6    Prevost, S.7    Schreiber, F.8
  • 34
    • 74049110959 scopus 로고    scopus 로고
    • The importance of protein-protein interactions on the pH-induced conformational changes of bovine serum albumin: a small-angle X-ray scattering study
    • Barbosa L.R.S., Ortore M.G., Spinozzi F., Mariani P., Bernstorff S., Itri R. The importance of protein-protein interactions on the pH-induced conformational changes of bovine serum albumin: a small-angle X-ray scattering study. Biophys J 2010, 98:147-157.
    • (2010) Biophys J , vol.98 , pp. 147-157
    • Barbosa, L.R.S.1    Ortore, M.G.2    Spinozzi, F.3    Mariani, P.4    Bernstorff, S.5    Itri, R.6
  • 35
    • 33847119938 scopus 로고    scopus 로고
    • Protein interactions studied by SAXS: effect of ionic strength and protein concentration for BSA in aqueous solutions
    • Zhang F.J., Skoda M.W.A., Jacobs R.M.J., Martin R.A., Martin C.M., Schreiber F. Protein interactions studied by SAXS: effect of ionic strength and protein concentration for BSA in aqueous solutions. J Phys Chem B 2007, 111:251-259.
    • (2007) J Phys Chem B , vol.111 , pp. 251-259
    • Zhang, F.J.1    Skoda, M.W.A.2    Jacobs, R.M.J.3    Martin, R.A.4    Martin, C.M.5    Schreiber, F.6
  • 37
    • 79951486635 scopus 로고    scopus 로고
    • Versatile application of indirect Fourier transformation to structure factor analysis: from X-ray diffraction of molecular liquids to small angle scattering of protein solutions
    • Fukasawa T., Sato T. Versatile application of indirect Fourier transformation to structure factor analysis: from X-ray diffraction of molecular liquids to small angle scattering of protein solutions. Phys Chem Chem Phys 2011, 13:3187-3196.
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 3187-3196
    • Fukasawa, T.1    Sato, T.2
  • 38
    • 78651293238 scopus 로고    scopus 로고
    • Salt-dependent DNA-DNA spacings in intact bacteriophage λ reflect relative importance of DNA self-repulsion and bending energies
    • Qiu X., Rau D.C., Parsegian V.A., Fang L.T., Knobler C.M., Gelbart W.M. Salt-dependent DNA-DNA spacings in intact bacteriophage λ reflect relative importance of DNA self-repulsion and bending energies. Phys Rev Lett 2011, 106:028102.
    • (2011) Phys Rev Lett , vol.106 , pp. 028102
    • Qiu, X.1    Rau, D.C.2    Parsegian, V.A.3    Fang, L.T.4    Knobler, C.M.5    Gelbart, W.M.6
  • 39
    • 84855672044 scopus 로고    scopus 로고
    • Cationic liposome-nucleic acid complexes: liquid crystal phases with applications in gene therapy
    • Safinya C.R., Ewert K.K., Leal C. Cationic liposome-nucleic acid complexes: liquid crystal phases with applications in gene therapy. Liq Cryst 2011, 38:1715-1723.
    • (2011) Liq Cryst , vol.38 , pp. 1715-1723
    • Safinya, C.R.1    Ewert, K.K.2    Leal, C.3
  • 41
    • 0031036238 scopus 로고    scopus 로고
    • Structure of DNA-cationic liposome complexes: DNA intercalation in multilamellar membranes in distinct interhelical packing regimes
    • Radler J.O., Koltover I., Salditt T., Safinya C.R. Structure of DNA-cationic liposome complexes: DNA intercalation in multilamellar membranes in distinct interhelical packing regimes. Science 1997, 275:810-814.
    • (1997) Science , vol.275 , pp. 810-814
    • Radler, J.O.1    Koltover, I.2    Salditt, T.3    Safinya, C.R.4
  • 42
    • 0032479572 scopus 로고    scopus 로고
    • An inverted hexagonal phase of cationic liposome-DNA complexes related to DNA release and delivery
    • Koltover I., Salditt T., Radler J.O., Safinya C.R. An inverted hexagonal phase of cationic liposome-DNA complexes related to DNA release and delivery. Science 1998, 281:78-81.
    • (1998) Science , vol.281 , pp. 78-81
    • Koltover, I.1    Salditt, T.2    Radler, J.O.3    Safinya, C.R.4
  • 45
    • 79959227621 scopus 로고    scopus 로고
    • The structure of ions and zwitterionic lipids regulates the charge of dipolar membranes
    • Szekely O., Steiner A., Szekely P., Amit E., Asor R., Tamburu C., Raviv U. The structure of ions and zwitterionic lipids regulates the charge of dipolar membranes. Langmuir 2011, 27:7419-7438.
    • (2011) Langmuir , vol.27 , pp. 7419-7438
    • Szekely, O.1    Steiner, A.2    Szekely, P.3    Amit, E.4    Asor, R.5    Tamburu, C.6    Raviv, U.7
  • 46
    • 79951471680 scopus 로고    scopus 로고
    • The role of calcium in membrane condensation and spontaneous curvature variations in model lipidic systems
    • Yaghmur A., Sartori B., Rappolt M. The role of calcium in membrane condensation and spontaneous curvature variations in model lipidic systems. Phys Chem Chem Phys 2011, 13:3115-3125.
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 3115-3125
    • Yaghmur, A.1    Sartori, B.2    Rappolt, M.3
  • 48
    • 84863926852 scopus 로고    scopus 로고
    • Structural evolution of environmentally responsive cationic liposome-DNA complexes with a reducible lipid linker
    • Shirazi R.S., Ewert K.K., Silva B.F.B., Leal C., Li Y.L., Safinya C.R. Structural evolution of environmentally responsive cationic liposome-DNA complexes with a reducible lipid linker. Langmuir 2012, 28:10495-10503.
    • (2012) Langmuir , vol.28 , pp. 10495-10503
    • Shirazi, R.S.1    Ewert, K.K.2    Silva, B.F.B.3    Leal, C.4    Li, Y.L.5    Safinya, C.R.6
  • 49
    • 79955909116 scopus 로고    scopus 로고
    • Two-dimensional packing of short DNA with nonpairing overhangs in cationic liposome-DNA complexes: from Onsager nematics to columnar nematics with finite-length columns
    • Bouxsein N.F., Leal C., McAllister C.S., Ewert K.K., Li Y.L., Samuel C.E., Safinya C.R. Two-dimensional packing of short DNA with nonpairing overhangs in cationic liposome-DNA complexes: from Onsager nematics to columnar nematics with finite-length columns. J Am Chem Soc 2011, 133:7585-7595.
    • (2011) J Am Chem Soc , vol.133 , pp. 7585-7595
    • Bouxsein, N.F.1    Leal, C.2    McAllister, C.S.3    Ewert, K.K.4    Li, Y.L.5    Samuel, C.E.6    Safinya, C.R.7
  • 50
    • 84865001035 scopus 로고    scopus 로고
    • Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system
    • Filippov S.K., Chytil P., Konarev P.V., Dyakonova M., Papadakis C.M., Zhigunov A., Plestil J., Stepanek P., Etrych T., Ulbrich K., et al. Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 2012, 13:2594-2604.
    • (2012) Biomacromolecules , vol.13 , pp. 2594-2604
    • Filippov, S.K.1    Chytil, P.2    Konarev, P.V.3    Dyakonova, M.4    Papadakis, C.M.5    Zhigunov, A.6    Plestil, J.7    Stepanek, P.8    Etrych, T.9    Ulbrich, K.10
  • 51
    • 78650260446 scopus 로고    scopus 로고
    • Molecular characterization of the interaction between siRNA and PAMAM G7 dendrimers by SAXS, ITC, and molecular dynamics simulations
    • Jensen L.B., Mortensen K., Pavan G.M., Kasimova M.R., Jensen D.K., Gadzhyeva V., Nielsen H.M., Foged C. Molecular characterization of the interaction between siRNA and PAMAM G7 dendrimers by SAXS, ITC, and molecular dynamics simulations. Biomacromolecules 2010, 11:3571-3577.
    • (2010) Biomacromolecules , vol.11 , pp. 3571-3577
    • Jensen, L.B.1    Mortensen, K.2    Pavan, G.M.3    Kasimova, M.R.4    Jensen, D.K.5    Gadzhyeva, V.6    Nielsen, H.M.7    Foged, C.8
  • 52
    • 79952711262 scopus 로고    scopus 로고
    • Synchrotron small angle X-ray scattering quantitatively detects angstrom level changes in the average radius of taxol-stabilized microtubules decorated with the microtubule-associated-protein tau
    • Choi Myung C., Raviv U., Li Y., Miller Herbert P., Needleman Daniel J., Kim Mahn W., Wilson L., Feinstein Stuart C., Safinya Cyrus R. Synchrotron small angle X-ray scattering quantitatively detects angstrom level changes in the average radius of taxol-stabilized microtubules decorated with the microtubule-associated-protein tau. J Phys Conf Ser 2011, 272:012001.
    • (2011) J Phys Conf Ser , vol.272 , pp. 012001
    • Choi Myung, C.1    Raviv, U.2    Li, Y.3    Miller Herbert, P.4    Needleman Daniel, J.5    Kim Mahn, W.6    Wilson, L.7    Feinstein Stuart, C.8    Safinya Cyrus, R.9
  • 55
    • 79953159140 scopus 로고    scopus 로고
    • Polymorphism of highly cross-linked F-actin networks: probing multiple length scales
    • Nguyen L.T., Hirst L.S. Polymorphism of highly cross-linked F-actin networks: probing multiple length scales. Phys Rev E 2011, 83.
    • (2011) Phys Rev E , pp. 83
    • Nguyen, L.T.1    Hirst, L.S.2
  • 56
    • 80053505075 scopus 로고    scopus 로고
    • Interaction strength between proteins and polyelectrolyte brushes: a small angle X-ray scattering study
    • Henzler K., Haupt B., Rosenfeldt S., Harnau L., Narayanan T., Ballauff M. Interaction strength between proteins and polyelectrolyte brushes: a small angle X-ray scattering study. Phys Chem Chem Phys 2011, 13:17599-17605.
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 17599-17605
    • Henzler, K.1    Haupt, B.2    Rosenfeldt, S.3    Harnau, L.4    Narayanan, T.5    Ballauff, M.6
  • 59
    • 79955571036 scopus 로고    scopus 로고
    • Development of a hard X-ray delay line for X-ray photon correlation spectroscopy and jitter-free pump-probe experiments at X-ray free-electron laser sources
    • Roseker W., Franz H., Schulte-Schrepping H., Ehnes A., Leupold O., Zontone F., Lee S., Robert A., Grubel G. Development of a hard X-ray delay line for X-ray photon correlation spectroscopy and jitter-free pump-probe experiments at X-ray free-electron laser sources. J Synchrotron Radiat 2011, 18:481-491.
    • (2011) J Synchrotron Radiat , vol.18 , pp. 481-491
    • Roseker, W.1    Franz, H.2    Schulte-Schrepping, H.3    Ehnes, A.4    Leupold, O.5    Zontone, F.6    Lee, S.7    Robert, A.8    Grubel, G.9
  • 60
    • 84867746860 scopus 로고    scopus 로고
    • Emerging opportunities in structural biology with X-ray free-electron lasers
    • Schlichting I., Miao J. Emerging opportunities in structural biology with X-ray free-electron lasers. Curr Opin Struct Biol 2012, 22:613-626.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 613-626
    • Schlichting, I.1    Miao, J.2
  • 61
    • 56549099844 scopus 로고    scopus 로고
    • Scatterless hybrid metal-single-crystal slit for small-angle X-ray scattering and high-resolution X-ray diffraction
    • Li Y.L., Beck R., Huang T., Choi M.C., Divinagracia M. Scatterless hybrid metal-single-crystal slit for small-angle X-ray scattering and high-resolution X-ray diffraction. J Appl Crystallogr 2008, 41:1134-1139.
    • (2008) J Appl Crystallogr , vol.41 , pp. 1134-1139
    • Li, Y.L.1    Beck, R.2    Huang, T.3    Choi, M.C.4    Divinagracia, M.5
  • 64
    • 34548008161 scopus 로고    scopus 로고
    • Phase-contrast X-ray imaging with a liquid-metal-jet-anode microfocus source
    • Tuohimaa T., Otendal M., Hertz H.M. Phase-contrast X-ray imaging with a liquid-metal-jet-anode microfocus source. Appl Phys Lett 2007, 91.
    • (2007) Appl Phys Lett , pp. 91
    • Tuohimaa, T.1    Otendal, M.2    Hertz, H.M.3
  • 67
    • 33845218265 scopus 로고    scopus 로고
    • Probing fast kinetics in complex fluids by combined rapid mixing and small-angle X-ray scattering
    • Panine P., Finet S., Weiss T.M., Narayanan T. Probing fast kinetics in complex fluids by combined rapid mixing and small-angle X-ray scattering. Adv Colloid Interface 2006, 127:9-18.
    • (2006) Adv Colloid Interface , vol.127 , pp. 9-18
    • Panine, P.1    Finet, S.2    Weiss, T.M.3    Narayanan, T.4
  • 70
    • 33847249296 scopus 로고    scopus 로고
    • Higher order assembly of microtubules by counter-ions: from hexagonal bundles to living necklaces
    • Needleman D.J., Ojeda-Lopez M.A., Raviv U., Miller H.P., Wilson L., Safinya C.R. Higher order assembly of microtubules by counter-ions: from hexagonal bundles to living necklaces. Biophys J 2005, 88:643a-644a.
    • (2005) Biophys J , vol.88
    • Needleman, D.J.1    Ojeda-Lopez, M.A.2    Raviv, U.3    Miller, H.P.4    Wilson, L.5    Safinya, C.R.6
  • 71
  • 73
    • 70349316826 scopus 로고    scopus 로고
    • Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline
    • David G., Perez J. Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline. J Appl Crystallogr 2009, 42:892-900.
    • (2009) J Appl Crystallogr , vol.42 , pp. 892-900
    • David, G.1    Perez, J.2
  • 74
    • 84866299595 scopus 로고    scopus 로고
    • X-ray studies of biological matter in microfluidic environments
    • Köster S., Pfohl T. X-ray studies of biological matter in microfluidic environments. Mod Phys Lett B 2012, 26:1230018.
    • (2012) Mod Phys Lett B , vol.26 , pp. 1230018
    • Köster, S.1    Pfohl, T.2
  • 78
    • 84867742972 scopus 로고    scopus 로고
    • Advances in X-ray scattering: from solution SAXS to achievements with coherent beams
    • Pérez J., Nishino Y. Advances in X-ray scattering: from solution SAXS to achievements with coherent beams. Curr Opin Struct Biol 2012, 22:670-678.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 670-678
    • Pérez, J.1    Nishino, Y.2
  • 82
    • 0034680144 scopus 로고    scopus 로고
    • Potential for biomolecular imaging with femtosecond X-ray pulses
    • Neutze R., Wouts R., van der Spoel D., Weckert E., Hajdu J. Potential for biomolecular imaging with femtosecond X-ray pulses. Nature 2000, 406:752-757.
    • (2000) Nature , vol.406 , pp. 752-757
    • Neutze, R.1    Wouts, R.2    van der Spoel, D.3    Weckert, E.4    Hajdu, J.5
  • 86
    • 83455210803 scopus 로고    scopus 로고
    • Three-dimensional technique on trial
    • Reich E.S. Three-dimensional technique on trial. Nature 2011, 480:303.
    • (2011) Nature , vol.480 , pp. 303
    • Reich, E.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.