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Volumn 5, Issue , 2014, Pages

Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography

(37)  Weierstall, Uwe a   James, Daniel a   Wang, Chong b   White, Thomas A c   Wang, Dingjie a   Liu, Wei b   Spence, John C H a   Bruce Doak, R a   Nelson, Garrett a   Fromme, Petra a   Fromme, Raimund a   Grotjohann, Ingo a   Kupitz, Christopher a   Zatsepin, Nadia A a   Liu, Haiguang a   Basu, Shibom a   Wacker, Daniel b   Won Han, Gye b   Katritch, Vsevolod b   Boutet, Sébastien d   more..

c DESY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; LIPID; MEMBRANE PROTEIN;

EID: 84894037590     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4309     Document Type: Article
Times cited : (462)

References (42)
  • 2
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • DOI 10.1110/ps.04712004
    • White, S. H. The progress of membrane protein structure determination. Protein Sci. 13, 1948-1949 (2004 (Pubitemid 38822136)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1948-1949
    • White, S.H.1
  • 3
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 resolution
    • DOI 10.1038/318618a0
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution. Nature 318, 618-624 (1985 (Pubitemid 16172409)
    • (1985) Nature , vol.318 , Issue.6047 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3
  • 4
    • 69949132434 scopus 로고    scopus 로고
    • Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10 mm size x-ray synchrotron beam
    • Cherezov, V. et al. Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10 mm size X-ray synchrotron beam. J. R. Soc. Interface 6, S587-S597 (2009
    • (2009) J. R. Soc. Interface , vol.6
    • Cherezov, V.1
  • 6
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • DOI 10.1126/science.277.5332.1676
    • Pebay-Peyroula, E. X-ray structure of Bacteriorhodopsin at 2.5 Angstroms from microcrystals grown in lipidic cubic phases. Science 277, 1676-1681 (1997 (Pubitemid 27446232)
    • (1997) Science , vol.277 , Issue.5332 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 7
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human 2-Adrenergic g protein coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human 2-Adrenergic G protein coupled receptor. Science 318, 1258 (2007
    • (2007) Science , vol.318 , pp. 1258
    • Cherezov, V.1
  • 8
    • 84871124956 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated K channel pore module in a closed state in lipid membranes
    • Santos, J. S. et al. Crystal structure of a voltage-gated K channel pore module in a closed state in lipid membranes. J. Biol. Chem. 287, 43063-43070 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 43063-43070
    • Santos, J.S.1
  • 9
    • 84863012221 scopus 로고    scopus 로고
    • Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger
    • Liao, J. et al. Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger. Science 335, 686-690 (2012
    • (2012) Science , vol.335 , pp. 686-690
    • Liao, J.1
  • 10
    • 84878145235 scopus 로고    scopus 로고
    • Crystal structure of the integral membrane diacylglycerol kinase
    • Li, D. et al. Crystal structure of the integral membrane diacylglycerol kinase. Nature 497, 521-524 (2013
    • (2013) Nature , vol.497 , pp. 521-524
    • Li, D.1
  • 11
    • 80052089906 scopus 로고    scopus 로고
    • Lipidic cubic phase technologies for membrane protein structural studies
    • Cherezov, V. Lipidic cubic phase technologies for membrane protein structural studies. Curr. Opin. Struc. Biol. 21, 559-566 (2011
    • (2011) Curr. Opin. Struc. Biol , vol.21 , pp. 559-566
    • Cherezov, V.1
  • 13
    • 77950813607 scopus 로고    scopus 로고
    • Radiation damage in macromolecular crystallography: What is it and why should we care
    • Garman, EF. Radiation damage in macromolecular crystallography: What is it and why should we care? Acta Cryst. D 66, 339-351 (2010
    • (2010) Acta Cryst , vol.D66 , pp. 339-351
    • Garman, E.F.1
  • 14
    • 84866315674 scopus 로고    scopus 로고
    • X-ray lasers for structural and dynamic biology
    • Spence, J., Weierstall, U. & Chapman, H. X-ray lasers for structural and dynamic biology. Rep. Prog. Phys. 75, 102601 (2012
    • (2012) Rep. Prog. Phys , vol.75 , pp. 102601
    • Spence, J.1    Weierstall, U.2    Chapman, H.3
  • 15
    • 80052103348 scopus 로고    scopus 로고
    • Femtosecond nanocrystallography using X-ray lasers for membrane protein structure determination
    • Fromme, P. & Spence, J. C. Femtosecond nanocrystallography using X-ray lasers for membrane protein structure determination. Curr. Opin. Struc. Biol. 21, 509-516 (2011
    • (2011) Curr. Opin. Struc. Biol , vol.21 , pp. 509-516
    • Fromme, P.1    Spence, J.C.2
  • 16
    • 79951594732 scopus 로고    scopus 로고
    • Phasing of coherent femtosecond X-ray diffraction from size-varying nanocrystals
    • Spence, J. C. H. et al. Phasing of coherent femtosecond X-ray diffraction from size-varying nanocrystals. Opt. Express. 19, 2866 (2011
    • (2011) Opt. Express , vol.19 , pp. 2866
    • Spence, J.C.H.1
  • 17
    • 79551658540 scopus 로고    scopus 로고
    • Femtosecond X-ray protein nanocrystallography
    • Chapman, H. N. et al. Femtosecond X-ray protein nanocrystallography. Nature 470, 73-77 (2011
    • (2011) Nature , vol.470 , pp. 73-77
    • Chapman, H.N.1
  • 18
    • 84862777982 scopus 로고    scopus 로고
    • Lipidic phase membrane protein serial femtosecond crystallography
    • Johansson, L. C. et al. Lipidic phase membrane protein serial femtosecond crystallography. Nat. Methods 9, 263-265 (2012
    • (2012) Nat. Methods , vol.9 , pp. 263-265
    • Johansson, L.C.1
  • 19
    • 84864004802 scopus 로고    scopus 로고
    • High-resolution protein structure determination by serial femtosecond crystallography
    • Boutet, S. et al. High-resolution protein structure determination by serial femtosecond crystallography. Science 337, 362-364 (2012
    • (2012) Science , vol.337 , pp. 362-364
    • Boutet, S.1
  • 20
    • 84872148917 scopus 로고    scopus 로고
    • Natively inhibited trypanosoma brucei cathepsin B structure determined by using an X-ray laser
    • Redecke, L. et al. Natively inhibited trypanosoma brucei cathepsin B structure determined by using an X-ray laser. Science 339, 227-230 (2013
    • (2013) Science , vol.339 , pp. 227-230
    • Redecke, L.1
  • 21
    • 53449087721 scopus 로고    scopus 로고
    • Gas dynamic virtual nozzle for generation of microscopic droplet streams
    • DePonte, D. P. et al. Gas dynamic virtual nozzle for generation of microscopic droplet streams. J. Phys. D. Appl. Phys. 41, 195505 (2008
    • (2008) J. Phys D. Appl. Phys , vol.41 , pp. 195505
    • DePonte, D.P.1
  • 23
    • 84890840505 scopus 로고    scopus 로고
    • Serial femtosecond crystallography of G protein-coupled receptors
    • Liu, W. et al. Serial femtosecond crystallography of G protein-coupled receptors. Science 342, 1521-1524 (2013
    • (2013) Science , vol.342 , pp. 1521-1524
    • Liu, W.1
  • 24
    • 84878112106 scopus 로고    scopus 로고
    • Structure of the human smoothened receptor bound to an antitumour agent
    • Wang, C. et al. Structure of the human smoothened receptor bound to an antitumour agent. Nature 497, 338-343 (2013
    • (2013) Nature , vol.497 , pp. 338-343
    • Wang, C.1
  • 25
    • 0034738979 scopus 로고    scopus 로고
    • Effects of oncogenic mutations in smoothened and patched can be reversed by cyclopamine
    • Taipale, J. et al. Effects of oncogenic mutations in smoothened and patched can be reversed by cyclopamine. Nature 406, 1005-1009 (2000
    • (2000) Nature , vol.406 , pp. 1005-1009
    • Taipale, J.1
  • 26
    • 84861602614 scopus 로고    scopus 로고
    • Injector for scattering measurements on fully solvated biospecies
    • Weierstall, U., Spence, J. C. H. & Doak, R. B. Injector for scattering measurements on fully solvated biospecies. Rev. Sci. Instrum. 83, 035108-035108 (2012
    • (2012) Rev. Sci. Instrum , vol.83 , pp. 035108-035108
    • Weierstall, U.1    Spence, J.C.H.2    Doak, R.B.3
  • 27
    • 83555178082 scopus 로고    scopus 로고
    • Wall slip of molten polymers
    • Hatzikiriakos, S. G. Wall slip of molten polymers. Prog. Polym. Sci 37, 624-643 (2012
    • (2012) Prog. Polym. Sci , vol.37 , pp. 624-643
    • Hatzikiriakos, S.G.1
  • 29
    • 84861961427 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of GPCRs by sodium ions
    • Liu, W. et al. Structural basis for allosteric regulation of GPCRs by sodium ions. Science 337, 232-236 (2012
    • (2012) Science , vol.337 , pp. 232-236
    • Liu, W.1
  • 30
    • 84877631485 scopus 로고    scopus 로고
    • Structural features for functional selectivity at serotonin receptors
    • Wacker, D. et al. Structural features for functional selectivity at serotonin receptors. Science 340, 615-619 (2013
    • (2013) Science , vol.340 , pp. 615-619
    • Wacker, D.1
  • 31
    • 84881193006 scopus 로고    scopus 로고
    • Structure of the human glucagon class B G-protein-coupled receptor
    • Siu, F. Y. et al. Structure of the human glucagon class B G-protein-coupled receptor. Nature 499, 444-449 (2013
    • (2013) Nature , vol.499 , pp. 444-449
    • Siu, F.Y.1
  • 32
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic mesophases. Nat. Protoc. 4, 706-731 (2009
    • (2009) Nat. Protoc , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 33
    • 75649119689 scopus 로고    scopus 로고
    • Nonlinear optical imaging of integral membrane protein crystals in lipidic mesophases
    • Kissick, D. J., Gualtieri, E. J., Simpson, G. J. & Cherezov, V. Nonlinear optical imaging of integral membrane protein crystals in lipidic mesophases. Anal. Chem. 82, 491 (2010
    • (2010) Anal. Chem , vol.82 , pp. 491
    • Kissick, D.J.1    Gualtieri, E.J.2    Simpson, G.J.3    Cherezov, V.4
  • 34
    • 84861984672 scopus 로고    scopus 로고
    • Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors
    • Chun, E. et al. Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors. Structure. 20, 967-976 (2012
    • (2012) Structure , vol.20 , pp. 967-976
    • Chun, E.1
  • 35
    • 77951528706 scopus 로고    scopus 로고
    • The coherent x-ray imaging (cxi) instrument at the linac coherent light source (lcls
    • Boutet, S. & Williams, G. J. The coherent X-ray imaging (CXI) instrument at the linac coherent light source (LCLS). New J. Phys. 12, 035024 (2010
    • (2010) New J. Phys , vol.12 , pp. 035024
    • Boutet, S.1    Williams, G.J.2
  • 36
    • 84879345494 scopus 로고    scopus 로고
    • Crystallographic data processing for free-electron laser sources
    • White, T. A. et al. Crystallographic data processing for free-electron laser sources. Acta Cryst. D 69, 1231-1240 (2013
    • (2013) Acta Cryst , vol.D69 , pp. 1231-1240
    • White, T.A.1
  • 37
    • 84859777150 scopus 로고    scopus 로고
    • Crystfel: A software suite for snapshot serial crystallography
    • White, T. A. et al. CrystFEL: A software suite for snapshot serial crystallography. J. Appl. Crystallogr. 45, 335-341 (2012
    • (2012) J. Appl. Crystallogr , vol.45 , pp. 335-341
    • White, T.A.1
  • 38
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • Mccoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • Mccoy, A.J.1
  • 39
    • 76449098262 scopus 로고    scopus 로고
    • Phenix: A comprehensive python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Cryst. D 66, 213-221 (2010
    • (2010) Acta Cryst , vol.D66 , pp. 213-221
    • Adams, P.D.1
  • 41
    • 0036829397 scopus 로고    scopus 로고
    • Inhibition of Hedgehog signaling by direct binding of cyclopamine to Smoothened
    • DOI 10.1101/gad.1025302
    • Chen, J. K., Taipale, J., Cooper, M. K. & Beachy, P. A. Inhibition of Hedgehog signaling by direct binding of cyclopamine to Smoothened. Genes Dev. 16, 2743-2748 (2002 (Pubitemid 35253140)
    • (2002) Genes and Development , vol.16 , Issue.21 , pp. 2743-2748
    • Chen, J.K.1    Taipale, J.2    Cooper, M.K.3    Beachy, P.A.4
  • 42
    • 74549178560 scopus 로고    scopus 로고
    • Molprobity: All-Atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: All-Atom structure validation for macromolecular crystallography. Acta Cryst. D 66, 12-21 (2009
    • (2009) Acta Cryst , vol.D66 , pp. 12-21
    • Chen, V.B.1


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