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Volumn 22, Issue 5, 2012, Pages 651-659

Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; MEMBRANE PROTEIN; MYOGLOBIN; PROTEIN;

EID: 84867743209     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2012.08.006     Document Type: Review
Times cited : (144)

References (75)
  • 1
    • 77954655410 scopus 로고    scopus 로고
    • Ultrafast X-ray scattering: structural dynamics from diatomic to protein molecules
    • Ihee H., Wulff M., Kim J., Adachi S Ultrafast X-ray scattering: structural dynamics from diatomic to protein molecules. Int Rev Phys Chem 2010, 29:453-520.
    • (2010) Int Rev Phys Chem , vol.29 , pp. 453-520
    • Ihee, H.1    Wulff, M.2    Kim, J.3    Adachi, S.4
  • 6
    • 0037007621 scopus 로고    scopus 로고
    • The challenge offered by X-ray lasers
    • Hajdu J. The challenge offered by X-ray lasers. Nature 2002, 417:15.
    • (2002) Nature , vol.417 , pp. 15
    • Hajdu, J.1
  • 7
    • 0024528771 scopus 로고
    • Time-resolved macromolecular crystallography
    • Moffat K. Time-resolved macromolecular crystallography. Annu Rev Biophys Biophys Chem 1989, 18:309-332.
    • (1989) Annu Rev Biophys Biophys Chem , vol.18 , pp. 309-332
    • Moffat, K.1
  • 11
    • 33646755415 scopus 로고    scopus 로고
    • Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin
    • Knapp J.E., Pahl R., Srajer V., Royer W.E. Allosteric action in real time: time-resolved crystallographic studies of a cooperative dimeric hemoglobin. Proc Natl Acad Sci U S A 2006, 103:7649-7654.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7649-7654
    • Knapp, J.E.1    Pahl, R.2    Srajer, V.3    Royer, W.E.4
  • 13
    • 0035923399 scopus 로고    scopus 로고
    • A molecular movie at 1.8Å resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds
    • Ren Z., Perman B., Srajer V., Teng T.Y., Pradervand C., Bourgeois D., Schotte F., Ursby T., Kort R., Wulff M., Moffat K. A molecular movie at 1.8Å resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds. Biochemistry 2001, 40:13788-13801.
    • (2001) Biochemistry , vol.40 , pp. 13788-13801
    • Ren, Z.1    Perman, B.2    Srajer, V.3    Teng, T.Y.4    Pradervand, C.5    Bourgeois, D.6    Schotte, F.7    Ursby, T.8    Kort, R.9    Wulff, M.10    Moffat, K.11
  • 16
  • 19
  • 21
    • 84988223602 scopus 로고    scopus 로고
    • Cooperative macromolecular device revealed by meta-analysis of static and time-resolved structures
    • Ren Z., Srajer V., Knapp J.E., Royer W.E. Cooperative macromolecular device revealed by meta-analysis of static and time-resolved structures. Proc Natl Acad Sci U S A 2012, 109:107-112.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 107-112
    • Ren, Z.1    Srajer, V.2    Knapp, J.E.3    Royer, W.E.4
  • 22
    • 1942469425 scopus 로고    scopus 로고
    • Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center
    • Baxter R.H., Ponomarenko N., Srajer V., Pahl R., Moffat K., Norris J.R. Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center. Proc Natl Acad Sci U S A 2004, 101:5982-5987.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5982-5987
    • Baxter, R.H.1    Ponomarenko, N.2    Srajer, V.3    Pahl, R.4    Moffat, K.5    Norris, J.R.6
  • 24
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer
    • Stowell M.H., McPhillips T.M., Rees D.C., Soltis S.M., Abresch E., Feher G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science 1997, 276:812-816.
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 25
    • 70350074909 scopus 로고    scopus 로고
    • Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface
    • Wohri A.B., Wahlgren W.Y., Malmerberg E., Johansson L.C., Neutze R., Katona G. Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface. Biochemistry 2009, 48:9831-9838.
    • (2009) Biochemistry , vol.48 , pp. 9831-9838
    • Wohri, A.B.1    Wahlgren, W.Y.2    Malmerberg, E.3    Johansson, L.C.4    Neutze, R.5    Katona, G.6
  • 31
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S., Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 2000, 406:653-657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 34
    • 84863168385 scopus 로고    scopus 로고
    • Protein structural dynamics of photoactive yellow protein in solution revealed by pump-probe X-ray solution scattering
    • Kim T.W., Lee J.H., Choi J., Kim K.H., van Wilderen L.J., Guerin L., Kim Y., Jung Y.O., Yang C., Kim J., et al. Protein structural dynamics of photoactive yellow protein in solution revealed by pump-probe X-ray solution scattering. J Am Chem Soc 2012, 134:3145-3153.
    • (2012) J Am Chem Soc , vol.134 , pp. 3145-3153
    • Kim, T.W.1    Lee, J.H.2    Choi, J.3    Kim, K.H.4    van Wilderen, L.J.5    Guerin, L.6    Kim, Y.7    Jung, Y.O.8    Yang, C.9    Kim, J.10
  • 35
    • 33744912217 scopus 로고    scopus 로고
    • Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy
    • Yeremenko S., van Stokkum I.H., Moffat K., Hellingwerf K.J. Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy. Biophys J 2006, 90:4224-4235.
    • (2006) Biophys J , vol.90 , pp. 4224-4235
    • Yeremenko, S.1    van Stokkum, I.H.2    Moffat, K.3    Hellingwerf, K.J.4
  • 36
    • 84860347602 scopus 로고    scopus 로고
    • Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100ps to 10ms with pump-probe X-ray solution scattering
    • Kim K.H., Muniyappan S., Oang K.Y., Kim J.G., Nozawa S., Sato T., Koshihara S.Y., Henning R., Kosheleva I., Ki H., et al. Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100ps to 10ms with pump-probe X-ray solution scattering. J Am Chem Soc 2012, 134:7001-7008.
    • (2012) J Am Chem Soc , vol.134 , pp. 7001-7008
    • Kim, K.H.1    Muniyappan, S.2    Oang, K.Y.3    Kim, J.G.4    Nozawa, S.5    Sato, T.6    Koshihara, S.Y.7    Henning, R.8    Kosheleva, I.9    Ki, H.10
  • 37
    • 79952337115 scopus 로고    scopus 로고
    • Anisotropic picosecond X-ray solution scattering from photo-selectively aligned protein molecules
    • Kim J., Kim K.H., Kim J.G., Kim T.W., Kim Y., Ihee H. Anisotropic picosecond X-ray solution scattering from photo-selectively aligned protein molecules. J Phys Chem Lett 2011, 2:350-356.
    • (2011) J Phys Chem Lett , vol.2 , pp. 350-356
    • Kim, J.1    Kim, K.H.2    Kim, J.G.3    Kim, T.W.4    Kim, Y.5    Ihee, H.6
  • 38
    • 78649811402 scopus 로고    scopus 로고
    • Direct observation of myoglobin structural dynamics from 100picoseconds to 1microsecond with picosecond X-ray solution scattering
    • Kim K.H., Oang K.Y., Kim J., Lee J.H., Kim Y., Ihee H. Direct observation of myoglobin structural dynamics from 100picoseconds to 1microsecond with picosecond X-ray solution scattering. Chem Commun 2011, 47:289-291.
    • (2011) Chem Commun , vol.47 , pp. 289-291
    • Kim, K.H.1    Oang, K.Y.2    Kim, J.3    Lee, J.H.4    Kim, Y.5    Ihee, H.6
  • 39
    • 70349679105 scopus 로고    scopus 로고
    • Protein tertiary structural changes visualized by time-resolved X-ray solution scattering
    • Ahn S., Kim K.H., Kim Y., Kim J., Ihee H. Protein tertiary structural changes visualized by time-resolved X-ray solution scattering. J Phys Chem B 2009, 113:13131-13133.
    • (2009) J Phys Chem B , vol.113 , pp. 13131-13133
    • Ahn, S.1    Kim, K.H.2    Kim, Y.3    Kim, J.4    Ihee, H.5
  • 43
    • 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
  • 57
    • 76749131505 scopus 로고    scopus 로고
    • Large-format, high-speed, X-ray pnCCDs combined with electron and ion imaging spectrometers in a multipurpose chamber for experiments at 4th generation light sources
    • Strüder L., Epp S., Rolles D., Hartmann R., Holl P., Lutz G., Soltau H., Eckart R., Reich C., Heinzinger K., et al. Large-format, high-speed, X-ray pnCCDs combined with electron and ion imaging spectrometers in a multipurpose chamber for experiments at 4th generation light sources. Nuc Inst Meth Phys Res A 2010, 614:483-496.
    • (2010) Nuc Inst Meth Phys Res A , vol.614 , pp. 483-496
    • Strüder, L.1    Epp, S.2    Rolles, D.3    Hartmann, R.4    Holl, P.5    Lutz, G.6    Soltau, H.7    Eckart, R.8    Reich, C.9    Heinzinger, K.10
  • 59
    • 0345305377 scopus 로고    scopus 로고
    • Diffraction imaging of single particles and biomolecules
    • Huldt G., Szoke A., Hajdu J. Diffraction imaging of single particles and biomolecules. J Struct Biol 2003, 144:219-227.
    • (2003) J Struct Biol , vol.144 , pp. 219-227
    • Huldt, G.1    Szoke, A.2    Hajdu, J.3
  • 60
    • 58149235114 scopus 로고    scopus 로고
    • Structure from fleeting illumination of faint spinning objects in flight
    • Fung R., Shneerson V., Saldin D.K., Ourmazd A. Structure from fleeting illumination of faint spinning objects in flight. Nat Phys 2009, 5:64-67.
    • (2009) Nat Phys , vol.5 , pp. 64-67
    • Fung, R.1    Shneerson, V.2    Saldin, D.K.3    Ourmazd, A.4
  • 61
    • 65649098443 scopus 로고    scopus 로고
    • AMO instrumentation for the LCLS X-ray FEL
    • Bozek J.D. AMO instrumentation for the LCLS X-ray FEL. Eur Phys J Spec Top 2009, 169:129-132.
    • (2009) Eur Phys J Spec Top , vol.169 , pp. 129-132
    • Bozek, J.D.1
  • 63
    • 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 Struct Biol 2011, 21:509-516.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 509-516
    • Fromme, P.1    Spence, J.C.2
  • 65
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 2006, 62:48-57.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 66
    • 0026853348 scopus 로고
    • Indexing in single-crystal diffractometry with an obstinate list of reflections
    • Duisenberg A.J.M. Indexing in single-crystal diffractometry with an obstinate list of reflections. J Appl Cryst 1992, 25:92-96.
    • (1992) J Appl Cryst , vol.25 , pp. 92-96
    • Duisenberg, A.J.M.1
  • 68
    • 77951528706 scopus 로고    scopus 로고
    • The coherent X-ray imaging (CXI) instrument at the linac coherent light source (LCLS)
    • Boutet S., Williams G.W. The coherent X-ray imaging (CXI) instrument at the linac coherent light source (LCLS). New J Phys 2010, 12:035024.
    • (2010) New J Phys , vol.12 , pp. 035024
    • Boutet, S.1    Williams, G.W.2
  • 70
    • 79952603450 scopus 로고    scopus 로고
    • New light on disordered ensembles: ab initio structure determination of one particle from scattering fluctuations of many copies
    • Saldin D.K., Poon H.C., Bogan M.J., Marchesini S., Shapiro D.A., Kirian R.A., Weierstall U., Spence J.C. New light on disordered ensembles: ab initio structure determination of one particle from scattering fluctuations of many copies. Phys Rev Lett 2011, 106:115501.
    • (2011) Phys Rev Lett , vol.106 , pp. 115501
    • Saldin, D.K.1    Poon, H.C.2    Bogan, M.J.3    Marchesini, S.4    Shapiro, D.A.5    Kirian, R.A.6    Weierstall, U.7    Spence, J.C.8
  • 73
    • 0032549731 scopus 로고    scopus 로고
    • Chemical dynamics in proteins: the photoisomerization of retinal in bacteriorhodopsin
    • Gai F., Hasson K.C., McDonald J.C., Anfinrud P.A. Chemical dynamics in proteins: the photoisomerization of retinal in bacteriorhodopsin. Science 1998, 279:1886-1891.
    • (1998) Science , vol.279 , pp. 1886-1891
    • Gai, F.1    Hasson, K.C.2    McDonald, J.C.3    Anfinrud, P.A.4
  • 74
    • 34248230651 scopus 로고    scopus 로고
    • Protein dynamics control the kinetics of initial electron transfer in photosynthesis
    • Wang H., Lin S., Allen J.P., Williams J.C., Blankert S., Laser C., Woodbury N.W. Protein dynamics control the kinetics of initial electron transfer in photosynthesis. Science 2007, 316:747-750.
    • (2007) Science , vol.316 , pp. 747-750
    • Wang, H.1    Lin, S.2    Allen, J.P.3    Williams, J.C.4    Blankert, S.5    Laser, C.6    Woodbury, N.W.7
  • 75
    • 78650885619 scopus 로고    scopus 로고
    • Engineered photoreceptors as novel optogenetic tools
    • Moeglich A., Moffat K. Engineered photoreceptors as novel optogenetic tools. Photochem Photobiol Sci 2010, 9:1286-1300.
    • (2010) Photochem Photobiol Sci , vol.9 , pp. 1286-1300
    • Moeglich, A.1    Moffat, K.2


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