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Volumn 27, Issue 1, 2014, Pages 24-31

Protein structure determination by MicroED

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; NANOCRYSTAL; PROTEIN; MEMBRANE PROTEIN;

EID: 84897494059     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.03.004     Document Type: Review
Times cited : (45)

References (40)
  • 4
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science 1997, 277:1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 8
    • 84888087327 scopus 로고    scopus 로고
    • Three-dimensional electron crystallography of protein microcrystals
    • Shi D., Nannenga B.L., Iadanza M.G., Gonen T. Three-dimensional electron crystallography of protein microcrystals. Elife 2013, 2.
    • (2013) Elife , pp. 2
    • Shi, D.1    Nannenga, B.L.2    Iadanza, M.G.3    Gonen, T.4
  • 9
    • 61449176982 scopus 로고    scopus 로고
    • Radiation damage in protein crystals examined under various conditions by different methods
    • Garman E.F., Nave C. Radiation damage in protein crystals examined under various conditions by different methods. J Synchrotron Radiat 2009, 16:129-132.
    • (2009) J Synchrotron Radiat , vol.16 , pp. 129-132
    • Garman, E.F.1    Nave, C.2
  • 10
    • 0028948565 scopus 로고
    • Radiation-damage in protein crystallography
    • Nave C. Radiation-damage in protein crystallography. Radiat Phys Chem 1995, 45:483-490.
    • (1995) Radiat Phys Chem , vol.45 , pp. 483-490
    • Nave, C.1
  • 12
    • 75749092651 scopus 로고    scopus 로고
    • Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures
    • Meents A., Gutmann S., Wagner A., Schulze-Briese C. Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures. Proc Natl Acad Sci U S A 2010, 107:1094-1099.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1094-1099
    • Meents, A.1    Gutmann, S.2    Wagner, A.3    Schulze-Briese, C.4
  • 14
    • 79551658540 scopus 로고    scopus 로고
    • Femtosecond X-ray protein nanocrystallography
    • The first proof of principle of structure determination from femtosecond X-ray crystallography where a hard-X-ray free-electron laser (XFEL) was used solve the 8.5 structure of photosystem I.
    • Chapman H.N., Fromme P., Barty A., White T.A., Kirian R.A., Aquila A., Hunter M.S., Schulz J., DePonte D.P., Weierstall U., et al. Femtosecond X-ray protein nanocrystallography. Nature 2011, 470:73-77. The first proof of principle of structure determination from femtosecond X-ray crystallography where a hard-X-ray free-electron laser (XFEL) was used solve the 8.5 structure of photosystem I.
    • (2011) Nature , vol.470 , pp. 73-77
    • Chapman, H.N.1    Fromme, P.2    Barty, A.3    White, T.A.4    Kirian, R.A.5    Aquila, A.6    Hunter, M.S.7    Schulz, J.8    DePonte, D.P.9    Weierstall, U.10
  • 16
    • 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
  • 20
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons electrons and X-rays for atomic-resolution microscopy of unstained biological molecules
    • Henderson R. The potential and limitations of neutrons electrons and X-rays for atomic-resolution microscopy of unstained biological molecules. Q Rev Biophys 1995, 28:171-193.
    • (1995) Q Rev Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 21
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature 1975, 257:28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 22
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin P.N., Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 1975, 94:425-440.
    • (1975) J Mol Biol , vol.94 , pp. 425-440
    • Unwin, P.N.1    Henderson, R.2
  • 23
    • 80054063377 scopus 로고    scopus 로고
    • Advances in structural and functional analysis of membrane proteins by electron crystallography
    • Wisedchaisri G., Reichow S.L., Gonen T. Advances in structural and functional analysis of membrane proteins by electron crystallography. Structure 2011, 19:1381-1393.
    • (2011) Structure , vol.19 , pp. 1381-1393
    • Wisedchaisri, G.1    Reichow, S.L.2    Gonen, T.3
  • 25
    • 0032545098 scopus 로고    scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum: merging electron diffraction tilt series and imaging the (h, k, 0) projection
    • 2+-ATPase from sarcoplasmic reticulum: merging electron diffraction tilt series and imaging the (h, k, 0) projection. J Mol Biol 1998, 284:1547-1564.
    • (1998) J Mol Biol , vol.284 , pp. 1547-1564
    • Shi, D.1    Lewis, M.R.2    Young, H.S.3    Stokes, D.L.4
  • 26
  • 27
    • 84879330227 scopus 로고    scopus 로고
    • A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals
    • Nederlof I., van Genderen E., Li Y.W., Abrahams J.P. A Medipix quantum area detector allows rotation electron diffraction data collection from submicrometre three-dimensional protein crystals. Acta Crystallogr D Biol Crystallogr 2013, 69:1223-1230.
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 1223-1230
    • Nederlof, I.1    van Genderen, E.2    Li, Y.W.3    Abrahams, J.P.4
  • 29
    • 84879775726 scopus 로고    scopus 로고
    • Overview of electron crystallography of membrane proteins: crystallization and screening strategies using negative stain electron microscopy
    • (Chapter 17: Unit17 15)
    • Nannenga B.L., Iadanza M.G., Vollmar B.S., Gonen T. Overview of electron crystallography of membrane proteins: crystallization and screening strategies using negative stain electron microscopy. Curr Protoc Protein Sci 2013, (Chapter 17: Unit17 15).
    • (2013) Curr Protoc Protein Sci
    • Nannenga, B.L.1    Iadanza, M.G.2    Vollmar, B.S.3    Gonen, T.4
  • 30
    • 84876033753 scopus 로고    scopus 로고
    • The collection of high-resolution electron diffraction data
    • Gonen T. The collection of high-resolution electron diffraction data. Methods Mol Biol 2013, 955:153-169.
    • (2013) Methods Mol Biol , vol.955 , pp. 153-169
    • Gonen, T.1
  • 31
    • 84901849376 scopus 로고    scopus 로고
    • A suite of software for processing microcrystal electron diffraction (MicroED) data
    • (submitted for publication)
    • Iadanza M.G., Gonen T. A suite of software for processing microcrystal electron diffraction (MicroED) data. Journal of Applied Crystallography 2014, (submitted for publication).
    • (2014) Journal of Applied Crystallography
    • Iadanza, M.G.1    Gonen, T.2
  • 35
    • 0029360316 scopus 로고
    • Diffuse scattering in electron diffraction data from protein crystals
    • Grigorieff N., Henderson R. Diffuse scattering in electron diffraction data from protein crystals. Ultramicroscopy 1995, 60:295-309.
    • (1995) Ultramicroscopy , vol.60 , pp. 295-309
    • Grigorieff, N.1    Henderson, R.2
  • 36
  • 37
    • 0000520380 scopus 로고
    • High-voltage electron-diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical
    • Glaeser R.M., Ceska T.A. High-voltage electron-diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical. Acta Crystallogr A 1989, 45:620-628.
    • (1989) Acta Crystallogr A , vol.45 , pp. 620-628
    • Glaeser, R.M.1    Ceska, T.A.2
  • 38
    • 33847168921 scopus 로고    scopus 로고
    • Structure solution with three-dimensional sets of processed electron diffraction intensities
    • Gemmi M., Nicolopoulos S. Structure solution with three-dimensional sets of processed electron diffraction intensities. Ultramicroscopy 2007, 107:483-494.
    • (2007) Ultramicroscopy , vol.107 , pp. 483-494
    • Gemmi, M.1    Nicolopoulos, S.2
  • 39
    • 84866340512 scopus 로고    scopus 로고
    • Structure characterization of hard materials by precession electron diffraction and automatic diffraction tomography: 6H-SiC semiconductor and Ni1+xTe1 embedded nanodomains
    • Sarakinou E., Mugnaioli E., Lioutas C.B., Vouroutzis N., Frangis N., Kolb U., Nikolopoulos S. Structure characterization of hard materials by precession electron diffraction and automatic diffraction tomography: 6H-SiC semiconductor and Ni1+xTe1 embedded nanodomains. Semicond Sci Technol 2012, 27.
    • (2012) Semicond Sci Technol , pp. 27
    • Sarakinou, E.1    Mugnaioli, E.2    Lioutas, C.B.3    Vouroutzis, N.4    Frangis, N.5    Kolb, U.6    Nikolopoulos, S.7
  • 40
    • 0011235329 scopus 로고    scopus 로고
    • Structure model for the phase AlmFe derived from three-dimensional electron diffraction intensity data collected by a precession technique. Comparison with convergent-beam diffraction
    • Gjonnes J., Hansen V., Berg B.S., Runde P., Cheng Y.F., Gjonnes K., Dorset D.L., Gilmore C.J. Structure model for the phase AlmFe derived from three-dimensional electron diffraction intensity data collected by a precession technique. Comparison with convergent-beam diffraction. Acta Crystallogr A 1998, 54:306-319.
    • (1998) Acta Crystallogr A , vol.54 , pp. 306-319
    • Gjonnes, J.1    Hansen, V.2    Berg, B.S.3    Runde, P.4    Cheng, Y.F.5    Gjonnes, K.6    Dorset, D.L.7    Gilmore, C.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.