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Volumn 34, Issue , 2015, Pages 87-98

Metalloprotein structures at ambient conditions and in real-time: Biological crystallography and spectroscopy using X-ray free electron lasers

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEIN; METAL; PROTEIN BINDING;

EID: 84940835264     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2015.07.014     Document Type: Review
Times cited : (41)

References (59)
  • 1
    • 84924266663 scopus 로고    scopus 로고
    • Radiation damage to macromolecules: kill or cure?
    • Garman E.F., Weik M. Radiation damage to macromolecules: kill or cure?. J Synchrotron Radiat 2015, 22:195-200.
    • (2015) J Synchrotron Radiat , vol.22 , pp. 195-200
    • Garman, E.F.1    Weik, M.2
  • 6
    • 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
  • 8
    • 79951870614 scopus 로고    scopus 로고
    • A simplified description of X-ray free-electron lasers
    • Margaritondo G., Rebernik Ribic P. A simplified description of X-ray free-electron lasers. J Synchrotron Radiat 2011, 18:101-108.
    • (2011) J Synchrotron Radiat , vol.18 , pp. 101-108
    • Margaritondo, G.1    Rebernik Ribic, P.2
  • 13
    • 84902478696 scopus 로고    scopus 로고
    • Enabling membrane protein structure and dynamics with X-ray free electron lasers
    • Feld G.K., Frank M. Enabling membrane protein structure and dynamics with X-ray free electron lasers. Curr Opin Struct Biol 2014, 27:69-78.
    • (2014) Curr Opin Struct Biol , vol.27 , pp. 69-78
    • Feld, G.K.1    Frank, M.2
  • 16
    • 84902668642 scopus 로고    scopus 로고
    • Liquid sample delivery techniques for serial femtosecond crystallography
    • Weierstall U. Liquid sample delivery techniques for serial femtosecond crystallography. Philos Trans R Soc Lond B Biol Sci 2014, 369:20130337.
    • (2014) Philos Trans R Soc Lond B Biol Sci , vol.369 , pp. 20130337
    • Weierstall, U.1
  • 24
    • 84875766495 scopus 로고    scopus 로고
    • X-ray free electron lasers motivate bioanalytical characterization of protein nanocrystals: serial femtosecond crystallography
    • Bogan M.J. X-ray free electron lasers motivate bioanalytical characterization of protein nanocrystals: serial femtosecond crystallography. Anal Chem 2013, 85:3464-3471.
    • (2013) Anal Chem , vol.85 , pp. 3464-3471
    • Bogan, M.J.1
  • 39
    • 84901819736 scopus 로고    scopus 로고
    • Cheetah: software for high-throughput reduction and analysis of serial femtosecond X-ray diffraction data
    • Barty A., Kirian R.A., Maia F.R., Hantke M., Yoon C.H., White T.A., Chapman H. Cheetah: software for high-throughput reduction and analysis of serial femtosecond X-ray diffraction data. J Appl Crystallogr 2014, 47:1118-1131.
    • (2014) J Appl Crystallogr , vol.47 , pp. 1118-1131
    • Barty, A.1    Kirian, R.A.2    Maia, F.R.3    Hantke, M.4    Yoon, C.H.5    White, T.A.6    Chapman, H.7
  • 43
    • 0025071357 scopus 로고
    • Cryoprotection of protein crystals against radiation damage in electron and x-ray diffraction
    • Henderson R. Cryoprotection of protein crystals against radiation damage in electron and x-ray diffraction. Proc R Soc London Ser B: Biol Sci 1990, 241:6-8.
    • (1990) Proc R Soc London Ser B: Biol Sci , vol.241 , pp. 6-8
    • Henderson, R.1
  • 47
    • 84899548497 scopus 로고    scopus 로고
    • 4Ca cluster in photosynthesis: where and how water is oxidized to dioxygen
    • 4Ca cluster in photosynthesis: where and how water is oxidized to dioxygen. Chem Rev 2014, 114:4175-4205.
    • (2014) Chem Rev , vol.114 , pp. 4175-4205
    • Yano, J.1    Yachandra, V.2
  • 48
    • 84881246012 scopus 로고    scopus 로고
    • Structural changes of the oxygen-evolving complex in photosystem II during the catalytic cycle
    • Glockner C., Kern J., Broser M., Zouni A., Yachandra V., Yano J. Structural changes of the oxygen-evolving complex in photosystem II during the catalytic cycle. J Biol Chem 2013, 288:22607-22620.
    • (2013) J Biol Chem , vol.288 , pp. 22607-22620
    • Glockner, C.1    Kern, J.2    Broser, M.3    Zouni, A.4    Yachandra, V.5    Yano, J.6
  • 49
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9Å
    • Umena Y., Kawakami K., Shen J.R., Kamiya N. Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9Å. Nature 2011, 473:55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 50
    • 11144306352 scopus 로고    scopus 로고
    • High resolution 1s core hole X-ray spectroscopy in 3d transition metal complexes-electronic and structural information
    • Glatzel P., Bergmann U. High resolution 1s core hole X-ray spectroscopy in 3d transition metal complexes-electronic and structural information. Coord Chem Rev 2005, 249:65-95.
    • (2005) Coord Chem Rev , vol.249 , pp. 65-95
    • Glatzel, P.1    Bergmann, U.2
  • 55
    • 84961291194 scopus 로고    scopus 로고
    • Simultaneous detection of electronic structure changes from two elements of a bifunctional catalyst using wavelength-dispersive X-ray emission spectroscopy and in situ electrochemistry
    • Gul S., Ng J.W., Alonso-Mori R., Kern J., Sokaras D., Anzenberg E., Lassalle-Kaiser B., Gorlin Y., Weng T.C., Zwart P.H., et al. Simultaneous detection of electronic structure changes from two elements of a bifunctional catalyst using wavelength-dispersive X-ray emission spectroscopy and in situ electrochemistry. Phys Chem Chem Phys 2015.
    • (2015) Phys Chem Chem Phys
    • Gul, S.1    Ng, J.W.2    Alonso-Mori, R.3    Kern, J.4    Sokaras, D.5    Anzenberg, E.6    Lassalle-Kaiser, B.7    Gorlin, Y.8    Weng, T.C.9    Zwart, P.H.10
  • 57
    • 84920181334 scopus 로고    scopus 로고
    • Resonant inelastic X-ray scattering on ferrous and ferric bis-imidazole porphyrin and cytochrome c: nature and role of the axial methionine-Fe bond
    • Kroll T., Hadt R.G., Wilson S.A., Lundberg M., Yan J.J., Weng T.C., Sokaras D., Alonso-Mori R., Casa D., Upton M.H., et al. Resonant inelastic X-ray scattering on ferrous and ferric bis-imidazole porphyrin and cytochrome c: nature and role of the axial methionine-Fe bond. J Am Chem Soc 2014, 136:18087-18099.
    • (2014) J Am Chem Soc , vol.136 , pp. 18087-18099
    • Kroll, T.1    Hadt, R.G.2    Wilson, S.A.3    Lundberg, M.4    Yan, J.J.5    Weng, T.C.6    Sokaras, D.7    Alonso-Mori, R.8    Casa, D.9    Upton, M.H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.