메뉴 건너뛰기




Volumn 10, Issue 2, 2004, Pages 261-269

A low-dose electron diffraction assay for protection of protein structure against damage from drying

Author keywords

Catalase; Electron crystallography; Electron diffraction; Polyvinylpyrrolidone; Protein structure; Resolution; Sugar sustains

Indexed keywords

CATALASE; DISACCHARIDE; ESTER; POVIDONE; SOLVENT;

EID: 2042427909     PISSN: 14319276     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1431927604040073     Document Type: Conference Paper
Times cited : (2)

References (41)
  • 1
    • 0026930092 scopus 로고
    • Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 kV electrons at near-atomic resolution
    • BRINK, J., CHIU, W. & DOUGHERTY, M. (1992). Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 kV electrons at near-atomic resolution. Ultramicrosc 46, 229-240.
    • (1992) Ultramicrosc , vol.46 , pp. 229-240
    • Brink, J.1    Chiu, W.2    Dougherty, M.3
  • 2
  • 3
    • 0036182386 scopus 로고    scopus 로고
    • Lessons from nature: The role of sugars in anhydrobiosis
    • CROWE, L.M. (2002). Lessons from nature: The role of sugars in anhydrobiosis. Comp Biochem Physiol 131A, 505-513.
    • (2002) Comp Biochem Physiol , vol.131 A , pp. 505-513
    • Crowe, L.M.1
  • 4
    • 0016230409 scopus 로고
    • The influence of dehydration on catalase stability. A comparison with freezing effects
    • DARBYSHIRE, B. (1974). The influence of dehydration on catalase stability. A comparison with freezing effects. Cryobiol 11, 148-151.
    • (1974) Cryobiol , vol.11 , pp. 148-151
    • Darbyshire, B.1
  • 5
    • 0032870614 scopus 로고    scopus 로고
    • Unexpected property of trehalose as observed by cryoelectron microscopy
    • DE CARLO, S., ADRIAN, M., KÄLIN, P., MAYER, J.M. & DUBOCHET, J. (1999). Unexpected property of trehalose as observed by cryoelectron microscopy. J Microsc (Oxf) 196, 40-45.
    • (1999) J Microsc (Oxf) , vol.196 , pp. 40-45
    • De Carlo, S.1    Adrian, M.2    Kälin, P.3    Mayer, J.M.4    Dubochet, J.5
  • 6
    • 0039841987 scopus 로고    scopus 로고
    • Accurate recording and measurement of electron diffraction data in structural and difference Fourier studies of proteins
    • DOWNING, K.H. & LI, H. (2001). Accurate recording and measurement of electron diffraction data in structural and difference Fourier studies of proteins. Microsc Microanal 7, 407-417.
    • (2001) Microsc Microanal , vol.7 , pp. 407-417
    • Downing, K.H.1    Li, H.2
  • 7
    • 0020220722 scopus 로고
    • The mounting of macromolecules for electron microscopy with particular reference to surface phenomena and the treatment of support films by glow discharge
    • DUBOCHET, J., GROOM, M. & MUELLER-NEUTEBOOM, S. (1982). The mounting of macromolecules for electron microscopy with particular reference to surface phenomena and the treatment of support films by glow discharge. Adv Optic Electron Microsc 8, 107-135.
    • (1982) Adv Optic Electron Microsc , vol.8 , pp. 107-135
    • Dubochet, J.1    Groom, M.2    Mueller-Neuteboom, S.3
  • 8
    • 0035144718 scopus 로고    scopus 로고
    • Structure analysis of soluble proteins using electron crystallography
    • ELLIS, M.J. & HEBERT, H. (2001). Structure analysis of soluble proteins using electron crystallography. Micron 32, 541-550.
    • (2001) Micron , vol.32 , pp. 541-550
    • Ellis, M.J.1    Hebert, H.2
  • 9
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • FRANK, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Ann Rev Biophys Biomol Struct 31, 303-319.
    • (2002) Ann Rev Biophys Biomol Struct , vol.31 , pp. 303-319
    • Frank, J.1
  • 10
    • 0033377941 scopus 로고    scopus 로고
    • Review: Electron crystallography: Present excitement, a nod to the past, anticipating the future
    • GLAESER, R.M. (1999). Review: Electron crystallography: Present excitement, a nod to the past, anticipating the future. J Struct Biol 128, 3-14.
    • (1999) J Struct Biol , vol.128 , pp. 3-14
    • Glaeser, R.M.1
  • 11
    • 13044262565 scopus 로고    scopus 로고
    • Complementing crystallography: The role of cryo-electron microscopy in structural biology
    • GRIMES, J.M., FULLER, S.D. & STUART, D.I. (1999) Complementing crystallography: The role of cryo-electron microscopy in structural biology. Acta Crystallogr D 55, 1742-1749.
    • (1999) Acta Crystallogr D , vol.55 , pp. 1742-1749
    • Grimes, J.M.1    Fuller, S.D.2    Stuart, D.I.3
  • 12
    • 17144427046 scopus 로고    scopus 로고
    • Negative stains containing trehalose: Application to tubular and filamentous structures
    • HARRIS, J.R., GERBER, M., GEBAUER, W., WERNICKE, W. & MARKL, J. (1996). Negative stains containing trehalose: Application to tubular and filamentous structures. J Microsc Soc Am 2, 43-52.
    • (1996) J Microsc Soc Am , vol.2 , pp. 43-52
    • Harris, J.R.1    Gerber, M.2    Gebauer, W.3    Wernicke, W.4    Markl, J.5
  • 13
    • 0036013787 scopus 로고    scopus 로고
    • Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: A review of applications
    • HARRIS, J.R. & SCHEFFLER, D. (2002). Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: A review of applications. Micron 33, 461-480.
    • (2002) Micron , vol.33 , pp. 461-480
    • Harris, J.R.1    Scheffler, D.2
  • 14
    • 0032695274 scopus 로고    scopus 로고
    • Trehalose embedding technique for high-resolution electron crystallography: Application to structural study of bacteriorhodopsin
    • HIRAI, T., MURATA, K., MITSUOKA, K., KIMURA, Y. & FUJIYOSHI, Y. (1999). Trehalose embedding technique for high-resolution electron crystallography: Application to structural study of bacteriorhodopsin. J Electron Microsc 48, 653-658.
    • (1999) J Electron Microsc , vol.48 , pp. 653-658
    • Hirai, T.1    Murata, K.2    Mitsuoka, K.3    Kimura, Y.4    Fujiyoshi, Y.5
  • 15
    • 0025297219 scopus 로고
    • Structure of PhoE porin in projection at 3.5Å resolution
    • JAP, B.K., DOWNING, K.H. & WALIAN, P.J. (1990). Structure of PhoE porin in projection at 3.5Å resolution. J Struct Biol 103, 57-63.
    • (1990) J Struct Biol , vol.103 , pp. 57-63
    • Jap, B.K.1    Downing, K.H.2    Walian, P.J.3
  • 16
    • 0033180259 scopus 로고    scopus 로고
    • Structure of orthorhombic crystals of beef liver catalase
    • KO, T.-P., DAY, J., MALKIN, A.J. & MCPHERSON, A. (1999). Structure of orthorhombic crystals of beef liver catalase. Acta Crystallogr D55, 1383-1394.
    • (1999) Acta Crystallogr , vol.D55 , pp. 1383-1394
    • Ko, T.-P.1    Day, J.2    Malkin, A.J.3    McPherson, A.4
  • 17
    • 0023660337 scopus 로고
    • Three-dimensional crystals of the light harvesting chlorophyll a/b protein complex from pea chloroplasts
    • KÜHLBRANDT, W. (1987). Three-dimensional crystals of the light harvesting chlorophyll a/b protein complex from pea chloroplasts. J Mol Biol 194, 757-762.
    • (1987) J Mol Biol , vol.194 , pp. 757-762
    • Kühlbrandt, W.1
  • 18
    • 0343620480 scopus 로고    scopus 로고
    • Analysis of macromolecular structure and dynamics by electron cryo-microscopy
    • KÜHLBRANDT, W. & WILLIAMS, K.A. (1999). Analysis of macromolecular structure and dynamics by electron cryo-microscopy. Curr Opin Chem Biol 3, 537-543.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 537-543
    • Kühlbrandt, W.1    Williams, K.A.2
  • 19
    • 85010252993 scopus 로고
    • The crystal structure of bovine liver catalase: A combined study by x-ray diffraction and electron microscopy
    • LONGLEY, W. (1967). The crystal structure of bovine liver catalase: A combined study by x-ray diffraction and electron microscopy. J Mol Biol 30, 323-327.
    • (1967) J Mol Biol , vol.30 , pp. 323-327
    • Longley, W.1
  • 20
    • 2042513470 scopus 로고
    • Potassium phosphate: An unconventional negative stain
    • Jouffrey, B. & Colliex, C. (Eds.), Les Ulis, France: Les Editions du Physique
    • MASSOVER, W.H. (1994). Potassium phosphate: An unconventional negative stain. In Electron Microscopy 1994, Jouffrey, B. & Colliex, C. (Eds.), pp. 569-570. Les Ulis, France: Les Editions du Physique.
    • (1994) Electron Microscopy 1994 , pp. 569-570
    • Massover, W.H.1
  • 21
    • 0035180498 scopus 로고    scopus 로고
    • Negative staining permits 4.0 Å resolution with low-dose electron diffraction of catalase crystals
    • MASSOVER, W.H., LAI, P.F. & MARSH, P. (2001). Negative staining permits 4.0 Å resolution with low-dose electron diffraction of catalase crystals. Ultramicrosc 90, 7-12.
    • (2001) Ultramicrosc , vol.90 , pp. 7-12
    • Massover, W.H.1    Lai, P.F.2    Marsh, P.3
  • 22
    • 0031238729 scopus 로고    scopus 로고
    • Heavy metals are not required for negative staining
    • MASSOVER, W.H. & MARSH, P. (1997). Heavy metals are not required for negative staining. Ultramicrosc 69, 139-150.
    • (1997) Ultramicrosc , vol.69 , pp. 139-150
    • Massover, W.H.1    Marsh, P.2
  • 23
    • 0034307901 scopus 로고    scopus 로고
    • Light atom derivatives of structures-preserving sugars are unconventional negative stains
    • MASSOVER, W.H. & MARSH, P. (2000). Light atom derivatives of structures-preserving sugars are unconventional negative stains. Ultramicrosc 85, 107-121.
    • (2000) Ultramicrosc , vol.85 , pp. 107-121
    • Massover, W.H.1    Marsh, P.2
  • 24
    • 0015518476 scopus 로고
    • Electron diffraction of wet proteins: Catalase
    • MATRICARDI, V.R., MORETZ, R.C. & PARSONS, D.F. (1972). Electron diffraction of wet proteins: Catalase. Science 177, 268-270.
    • (1972) Science , vol.177 , pp. 268-270
    • Matricardi, V.R.1    Moretz, R.C.2    Parsons, D.F.3
  • 25
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • MATTHEWS, B.W. (1968). Solvent content of protein crystals. J Mol Biol 33, 491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 26
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
    • MITSUOKA, K., HIRAI, T., MURATA, K., MIYAZAWA, A., KIDERA, A., KIMURA, Y. & FUJIYOSHI, Y. (1999). The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution. J Mol Biol 286, 861-882.
    • (1999) J Mol Biol , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 27
    • 0028856299 scopus 로고
    • Preservation of 2-D crystals of tubulin for electron crystallography
    • NOGALES, E., WOLF, S.G., ZHANG, S.X. & DOWNING, K.H. (1995). Preservation of 2-D crystals of tubulin for electron crystallography. J Struct Biol 115, 199-208.
    • (1995) J Struct Biol , vol.115 , pp. 199-208
    • Nogales, E.1    Wolf, S.G.2    Zhang, S.X.3    Downing, K.H.4
  • 29
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • PRESTRELSKI, S.J., TEDESCHI, N., ARAKAWA, T. & CARPENTER, J.F. (1993). Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys J 65, 661-671.
    • (1993) Biophys J , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 31
    • 0033776856 scopus 로고    scopus 로고
    • Macromolecular structure determination by cryo-electron microscopy
    • SAIBIL, H.R. (2000). Macromolecular structure determination by cryo-electron microscopy. Acta Crystallogr D 56, 1215-1222.
    • (2000) Acta Crystallogr D , vol.56 , pp. 1215-1222
    • Saibil, H.R.1
  • 32
    • 0025552735 scopus 로고
    • Zero-loss energy filtering as improved imaging mode in cryoelectron-microscopy of frozen-hydrated specimens
    • SCHROEDER, R.R., HOFMANN, W. & MÉNÉTRET, J.-F. (1990). Zero-loss energy filtering as improved imaging mode in cryoelectron-microscopy of frozen-hydrated specimens. J Struct Biol 105, 28-34.
    • (1990) J Struct Biol , vol.105 , pp. 28-34
    • Schroeder, R.R.1    Hofmann, W.2    Ménétret, J.-F.3
  • 33
    • 0030174932 scopus 로고    scopus 로고
    • Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures
    • STARK, H., ZEMLIN, F. & BOETTCHER, C. (1996). Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures. Ultramicrosc 63, 75-79.
    • (1996) Ultramicrosc , vol.63 , pp. 75-79
    • Stark, H.1    Zemlin, F.2    Boettcher, C.3
  • 34
    • 0032538131 scopus 로고    scopus 로고
    • Protein inactivation in amorphous sucrose and trehalose matrices: Effects of phase separation and crystallization
    • SUN, W.Q. & DAVIDSON, P. (1998). Protein inactivation in amorphous sucrose and trehalose matrices: Effects of phase separation and crystallization. Biochim Biophys Acta 1425, 235-244.
    • (1998) Biochim Biophys Acta , vol.1425 , pp. 235-244
    • Sun, W.Q.1    Davidson, P.2
  • 35
    • 0025817772 scopus 로고
    • Cryoprotective effect of saccharides on denaturation of catalase by freeze-drying
    • TANAKA, K., TAKEDA, T. & MIYAJIMA, K. (1991). Cryoprotective effect of saccharides on denaturation of catalase by freeze-drying. Chem Pharmaceut Bull 39, 1091-1094.
    • (1991) Chem Pharmaceut Bull , vol.39 , pp. 1091-1094
    • Tanaka, K.1    Takeda, T.2    Miyajima, K.3
  • 36
    • 0016697708 scopus 로고
    • Beef liver catalase structure: Interpretation of electron micrographs
    • UNWIN, P.N.T. (1975). Beef liver catalase structure: Interpretation of electron micrographs. J Mol Biol 98, 235-242.
    • (1975) J Mol Biol , vol.98 , pp. 235-242
    • Unwin, P.N.T.1
  • 37
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • UNWIN, P.N.T. & HENDERSON, R. (1975). Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 94, 425-440.
    • (1975) J Mol Biol , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 38
    • 0028922247 scopus 로고
    • Protective effect of disaccharides on restriction endonucleases during drying under vacuum
    • URITANI, M., TAKAI, M. & YOSHINAGA, K. (1995). Protective effect of disaccharides on restriction endonucleases during drying under vacuum. J Biochem 117, 774-779.
    • (1995) J Biochem , vol.117 , pp. 774-779
    • Uritani, M.1    Takai, M.2    Yoshinaga, K.3
  • 39
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • WANG, D.N. & KÜHLBRANDT, W. (1991). High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J Mol Biol 217, 691-699.
    • (1991) J Mol Biol , vol.217 , pp. 691-699
    • Wang, D.N.1    Kühlbrandt, W.2
  • 40
    • 0014328849 scopus 로고
    • The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy
    • WRIGLEY, N.G. (1968). The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy. J Ultrastruct Res 24, 454-464.
    • (1968) J Ultrastruct Res , vol.24 , pp. 454-464
    • Wrigley, N.G.1
  • 41
    • 0036229990 scopus 로고    scopus 로고
    • Quantitative comparison of zero-loss and conventional electron diffraction from two-dimensional and thin three-dimensional protein crystals
    • YONEKURA, K., MAKI-YONEKURA, S. & NAMBA K. (2002). Quantitative comparison of zero-loss and conventional electron diffraction from two-dimensional and thin three-dimensional protein crystals. Biophys J 82, 2784-2797.
    • (2002) Biophys J , vol.82 , pp. 2784-2797
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.