메뉴 건너뛰기




Volumn 369, Issue 1647, 2014, Pages

7 Å resolution in protein twodimensional-crystal X-ray diffraction at Linac Coherent Light Source

(25)  Pedrini, Bill a   Tsai, Ching Ju a   Capitani, Guido a   Padeste, Celestino a   Hunter, Mark S b   Zatsepin, Nadia A d   Barty, Anton e   Henry Benner, W b   Boutet, Sébastien f   Feld, Geoffrey K b   Hau Riege, Stefan P b   Kirian, Richard A e   Kupitz, Christopher d   Messerschmitt, Marc f   Ogren, John I g   Pardini, Tommaso b   Segelke, Brent b   Williams, Garth J f   Spence, John C H d   Abela, Rafael a   more..

e DESY   (Germany)

Author keywords

Bacteriorhodopsin; Crystallographic data analysis; Two dimensional protein crystal; X ray diffraction; X ray free electron laser

Indexed keywords

DATA PROCESSING; IMAGE RESOLUTION; LIPID; PROTEIN; TEMPERATURE EFFECT; X-RAY DIFFRACTION;

EID: 84902524259     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2013.0500     Document Type: Article
Times cited : (33)

References (24)
  • 1
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • (doi: 10. 1038/nature08144)
    • Rosenbaum DM, Rasmussen SGF, Kobilka BK. 2009 The structure and function of G-protein-coupled receptors. Nature 459, 356-363. (doi: 10. 1038/nature08144).
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 2
    • 84859311522 scopus 로고    scopus 로고
    • Conserved activation paths in G-protein-coupled receptors
    • (doi: 10. 1042/BST20120001)
    • Deupi X, Standfuss J, Schertler G. 2012 Conserved activation paths in G-protein-coupled receptors. Biochem. Soc. Trans. 40, 383-388. (doi: 10. 1042/BST20120001).
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 383-388
    • Deupi, X.1    Standfuss, J.2    Schertler, G.3
  • 3
    • 80052040244 scopus 로고    scopus 로고
    • Electron crystallography for structural and functional studies of membrane proteins
    • (doi: 10. 1093/jmicro/dfr008)
    • Fujiyoshi Y. 2011 Electron crystallography for structural and functional studies of membrane proteins. J. Electron Microsc. 60, S149-S159. (doi: 10. 1093/jmicro/dfr008).
    • (2011) J. Electron Microsc , vol.60
    • Fujiyoshi, Y.1
  • 4
    • 84863617793 scopus 로고    scopus 로고
    • Analysis of conformational variation in macromolecular structural models
    • (doi: 10. 1371/journal. pone. 0039993)
    • Srivastava SK, Gayathri S, Manjasetty BA, Gopal B. 2012 Analysis of conformational variation in macromolecular structural models. PLoS ONE 7, e39993. (doi: 10. 1371/journal. pone. 0039993).
    • (2012) PLoS ONE , vol.7
    • Srivastava, S.K.1    Gayathri, S.2    Manjasetty, B.A.3    Gopal, B.4
  • 5
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • (doi: 10. 1038/257028a0)
    • Unwin PNT, Henderson R. 1975 Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257, 28-32. (doi: 10. 1038/257028a0).
    • (1975) Nature , vol.257 , pp. 28-32
    • Unwin, P.N.T.1    Henderson, R.2
  • 6
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • (doi: 10. 1038/367614a0)
    • Kühlbrandt W, Wang DN, Fujiyoshi Y. 1994 Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614-621. (doi: 10. 1038/367614a0).
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 7
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • (doi: 10. 1038/362770a0)
    • Schertler G, Villa C, Henderson R. 1993 Projection structure of rhodopsin. Nature 362, 770-772. (doi: 10. 1038/362770a0).
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.1    Villa, C.2    Henderson, R.3
  • 8
    • 33751217140 scopus 로고    scopus 로고
    • On the nature of 2D crystal unbending
    • (doi: 10. 1016/j. jsb. 2006. 07. 012)
    • Gil D, Carazo JM, Marabini R. 2006 On the nature of 2D crystal unbending. J. Struct. Biol. 156, 546-555. (doi: 10. 1016/j. jsb. 2006. 07. 012).
    • (2006) J. Struct. Biol , vol.156 , pp. 546-555
    • Gil, D.1    Carazo, J.M.2    Marabini, R.3
  • 9
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • (doi: 10. 1016/0022-2836(75)90212-0)
    • Unwin PNT, Henderson R. 1975 Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94, 425-440. (doi: 10. 1016/0022-2836(75)90212-0).
    • (1975) J. Mol. Biol , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 10
    • 0025312416 scopus 로고
    • Analysis of highresolution electron diffraction patterns from purple membrane labelled with heavy-atoms
    • (doi: 10. 1016/S0022-2836(05) 80214-1)
    • Ceska TA, Henderson R. 1990 Analysis of highresolution electron diffraction patterns from purple membrane labelled with heavy-atoms. J. Mol. Biol. 213, 539-560. (doi: 10. 1016/S0022-2836(05) 80214-1).
    • (1990) J. Mol. Biol , vol.213 , pp. 539-560
    • Ceska, T.A.1    Henderson, R.2
  • 11
    • 0034712851 scopus 로고    scopus 로고
    • The three-dimensional structure of halorhodopsin to 5 Åby electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure
    • (doi: 10. 1073/pnas. 080064697)
    • Kunji ER, von Grunau S, Oesterhelt D, Henderson R. 2000 The three-dimensional structure of halorhodopsin to 5 Åby electron crystallography: a new unbending procedure for two-dimensional crystals by using a global reference structure. Proc. Natl Acad. Sci. USA 97, 4637-4642. (doi: 10. 1073/pnas. 080064697).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4637-4642
    • Kunji, E.R.1    von Grunau, S.2    Oesterhelt, D.3    Henderson, R.4
  • 12
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • (doi: 10. 1016/S0022-2836(05)80271-2)
    • Henderson R et al. 1990 Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899-929. (doi: 10. 1016/S0022-2836(05)80271-2).
    • (1990) J. Mol. Biol , vol.213 , pp. 899-929
    • Henderson, R.1
  • 13
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • (doi: 10. 1038/nature04321)
    • Gonen T et al. 2005 Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 438, 633-638. (doi: 10. 1038/nature04321).
    • (2005) Nature , vol.438 , pp. 633-638
    • Gonen, T.1
  • 14
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson R. 1995 The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. J. Mol. Biol. 28, 171-193.
    • (1995) J. Mol. Biol , vol.28 , pp. 171-193
    • Henderson, R.1
  • 15
    • 77956280553 scopus 로고    scopus 로고
    • First lasing and operation of an ångstrom-wavelength free-electron laser
    • (doi: 10. 1038/nphoton. 2010. 176)
    • Emma P et al. 2010 First lasing and operation of an ångstrom-wavelength free-electron laser. Nat. Photon. 4, 641-647. (doi: 10. 1038/nphoton. 2010. 176).
    • (2010) Nat. Photon , vol.4 , pp. 641-647
    • Emma, P.1
  • 16
    • 79960949598 scopus 로고    scopus 로고
    • X-rays: First light from SACLA
    • (doi: 10. 1038/nphoton. 2011. 178)
    • Pile D. 2011 X-rays: first light from SACLA. Nat. Photon. 5, 456-457. (doi: 10. 1038/nphoton. 2011. 178).
    • (2011) Nat. Photon , vol.5 , pp. 456-457
    • Pile, D.1
  • 17
    • 0016637383 scopus 로고
    • The structure of the purple membrane from Halobacterium halobium: Analysis of the X-ray diffraction pattern
    • (doi: 10. 1016/0022-2836(75)90123-0)
    • Henderson R. 1975 The structure of the purple membrane from Halobacterium halobium: analysis of the X-ray diffraction pattern. J. Mol. Biol. 93, 123-138. (doi: 10. 1016/0022-2836(75)90123-0).
    • (1975) J. Mol. Biol , vol.93 , pp. 123-138
    • Henderson, R.1
  • 18
    • 0033574505 scopus 로고    scopus 로고
    • X-ray diffraction from a single layer of purple membrane at the air/water interface
    • (doi: 10. 1006/jmbi. 1999. 2644)
    • Verclas SAW et al. 1999 X-ray diffraction from a single layer of purple membrane at the air/water interface. J. Mol. Biol. 287, 837-843. (doi: 10. 1006/jmbi. 1999. 2644).
    • (1999) J. Mol. Biol , vol.287 , pp. 837-843
    • Verclas, S.A.W.1
  • 19
    • 84864004802 scopus 로고    scopus 로고
    • High-resolution protein structure determination by serial femtosecond crystallography
    • (doi: 10. 1126/science. 1217737)
    • Boutet S et al. 2012 High-resolution protein structure determination by serial femtosecond crystallography. Science 337, 362-364. (doi: 10. 1126/science. 1217737).
    • (2012) Science , vol.337 , pp. 362-364
    • Boutet, S.1
  • 20
    • 0344552340 scopus 로고    scopus 로고
    • Three-dimensional diffractive imaging for crystalline monolayers with onedimensional compact support
    • (doi: 10. 1016/j. jsb. 2003. 09. 019)
    • Spence JCH, Weierstall U, Fricke TT, Glaeser RM, Downing KH. 2003 Three-dimensional diffractive imaging for crystalline monolayers with onedimensional compact support. J. Struct. Biol. 144, 209-218. (doi: 10. 1016/j. jsb. 2003. 09. 019).
    • (2003) J. Struct. Biol , vol.144 , pp. 209-218
    • Spence, J.C.H.1    Weierstall, U.2    Fricke, T.T.3    Glaeser, R.M.4    Downing, K.H.5
  • 21
    • 84902461168 scopus 로고    scopus 로고
    • Femtosecond X-ray diffraction from two-dimensional protein crystals
    • (doi: 10. 1107/S205225 2514001444)
    • Frank M et al. 2013 Femtosecond X-ray diffraction from two-dimensional protein crystals. Int. Union Crystallogr. J. 1, 95-100. (doi: 10. 1107/S205225 2514001444).
    • (2013) Int. Union Crystallogr. J , vol.1 , pp. 95-100
    • Frank, M.1
  • 22
    • 77951528706 scopus 로고    scopus 로고
    • The coherent X-ray imaging (CXI) instrument at the Linac Coherent Light Source (LCLS)
    • (doi: 10. 1088/1367-2630/12/3/035024)
    • Boutet S, Williams GJ. 2010 The coherent X-ray imaging (CXI) instrument at the Linac Coherent Light Source (LCLS). New J. Phys. 12, 035024. (doi: 10. 1088/1367-2630/12/3/035024).
    • (2010) New J. Phys , vol.12 , pp. 035024
    • Boutet, S.1    Williams, G.J.2
  • 23
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from twodimensional crystals
    • (doi: 10. 1016/0304-3991(84)90217-1)
    • Baldwin J, Henderson R. 1984 Measurement and evaluation of electron diffraction patterns from twodimensional crystals. Ultramicroscopy 14, 319-336. (doi: 10. 1016/0304-3991(84)90217-1).
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.1    Henderson, R.2
  • 24
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of the electron micrographs at 3. 5 Å resolution
    • (doi: 10. 1016/0304-3991(86)90203-2)
    • Henderson R, Baldwin JM, Downing KH, Lepault J, Zemlin F. 1990 Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of the electron micrographs at 3. 5 Å resolution. Ultramicroscopy 19, 147-178. (doi: 10. 1016/0304-3991(86)90203-2).
    • (1990) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.