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Volumn 343, Issue 5, 2004, Pages 1243-1254

Crystallization of transmembrane proteins in cubo: Mechanisms of crystal growth and defect formation

Author keywords

crystallization mechanisms; lipidic cubic phases; molecular resolution AFM; nucleation; transmembrane proteins

Indexed keywords

BACTERIORHODOPSIN; BUFFER; DETERGENT; MEMBRANE PROTEIN;

EID: 6344238642     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.022     Document Type: Article
Times cited : (41)

References (71)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • E. Wallin, and G. von Heijne Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms Protein Sci. 7 1998 1029 1038
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 2
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, and K.H. Downing Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy J. Mol. Biol. 213 1990 899 929
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 3
    • 0016842810 scopus 로고
    • Three dimensional model of purple membrane obtained by electron microscopy
    • R. Henderson, and P.N.T. Unwin Three dimensional model of purple membrane obtained by electron microscopy Nature 257 1975 28 32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 4
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • W. Kühlbrandt, D.N. Wang, and Y. Fujiyoshi Atomic model of plant light-harvesting complex by electron crystallography Nature 367 1994 614 621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 5
    • 0033380377 scopus 로고    scopus 로고
    • The structure of aquaporin-1 at 4.5-angstrom resolution reveals short alpha-helices in the center of the monomer
    • K. Mitsuoka, K. Murata, T. Walz, T. Hirai, P. Agre, and J.B. Heymann The structure of aquaporin-1 at 4.5-angstrom resolution reveals short alpha-helices in the center of the monomer J. Struct. Biol. 128 1999 34 43
    • (1999) J. Struct. Biol. , vol.128 , pp. 34-43
    • Mitsuoka, K.1    Murata, K.2    Walz, T.3    Hirai, T.4    Agre, P.5    Heymann, J.B.6
  • 6
    • 0034609808 scopus 로고    scopus 로고
    • Structural determinants of water permeation through aquaporin-1
    • K. Murata, K. Mitsuoka, T. Hirai, T. Walz, P. Agre, and J.B. Heymann Structural determinants of water permeation through aquaporin-1 Nature 407 2000 599 605
    • (2000) Nature , vol.407 , pp. 599-605
    • Murata, K.1    Mitsuoka, K.2    Hirai, T.3    Walz, T.4    Agre, P.5    Heymann, J.B.6
  • 7
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 angstrom resolution: Transverse tunnels in the channel wall
    • A. Miyazawa, Y. Fujiyoshi, M. Stowell, and N. Unwin Nicotinic acetylcholine receptor at 4.6 angstrom resolution: transverse tunnels in the channel wall J. Mol. Biol. 288 1999 765 786
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 8
    • 0035979768 scopus 로고    scopus 로고
    • Two-dimensional crystals: A powerful approach to assess structure, function and dynamics of membrane proteins
    • H. Stahlberg, D. Fotiadis, S. Scheuring, H. Remigy, T. Braun, and K. Mitsuoka Two-dimensional crystals: a powerful approach to assess structure, function and dynamics of membrane proteins FEBS Letters 504 2001 166 172
    • (2001) FEBS Letters , vol.504 , pp. 166-172
    • Stahlberg, H.1    Fotiadis, D.2    Scheuring, S.3    Remigy, H.4    Braun, T.5    Mitsuoka, K.6
  • 10
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • C. Hunte, and H. Michel Crystallisation of membrane proteins mediated by antibody fragments Curr. Opin. Struct. Biol. 12 2002 503 508
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 13
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • E. Pebay-Peyroula, G. Rummel, J.P. Rosenbusch, and E.M. Landau X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases Science 277 1997 1676 1681
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 16
    • 0242669292 scopus 로고    scopus 로고
    • Using rational screening and electron microscopy to optimize the crystallization of succinate: Ubiquinone oxidoreductase from Escherichia coli
    • R. Horsefield, V. Yankovskaya, S. Tornroth, C. Luna-Chavez, E. Stambouli, and J. Barber Using rational screening and electron microscopy to optimize the crystallization of succinate: ubiquinone oxidoreductase from Escherichia coli Acta Crystallog. sect. D 59 2003 600 602
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 600-602
    • Horsefield, R.1    Yankovskaya, V.2    Tornroth, S.3    Luna-Chavez, C.4    Stambouli, E.5    Barber, J.6
  • 17
    • 0034663616 scopus 로고    scopus 로고
    • Fusion protein approach to improve the crystal quality of cytochrome bo(3) ubiquinol oxidase from Escherichia coli
    • B. Byrne, J. Abramson, M. Jansson, E. Holmgren, and S. Iwata Fusion protein approach to improve the crystal quality of cytochrome bo(3) ubiquinol oxidase from Escherichia coli Biochim. Biophys. Acta-Bioenerg. 1459 2000 449 455
    • (2000) Biochim. Biophys. Acta-Bioenerg. , vol.1459 , pp. 449-455
    • Byrne, B.1    Abramson, J.2    Jansson, M.3    Holmgren, E.4    Iwata, S.5
  • 18
    • 0028890031 scopus 로고
    • Structure at 2.8-Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel Structure at 2.8-Å resolution of cytochrome c oxidase from Paracoccus denitrificans Nature 376 1995 660 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 19
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields monomeric bacteriorhodopsin structure
    • S. Faham, and J.U. Bowie Bicelle crystallization: a new method for crystallizing membrane proteins yields monomeric bacteriorhodopsin structure J. Mol. Biol. 316 2002 1 6
    • (2002) J. Mol. Biol. , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 20
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • E.M. Landau, and J.P. Rosenbusch Lipidic cubic phases: a novel concept for the crystallization of membrane proteins Proc. Natl Acad. Sci. USA 93 1996 14532 14535
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 21
    • 6344262470 scopus 로고    scopus 로고
    • Crystallization of membrane proteins in lipidic cubic phases
    • S. Iwata International University Line La Jolla, CA
    • E.M. Landau Crystallization of membrane proteins in lipidic cubic phases S. Iwata Methods and Results in Crystallization of Membrane Proteins 2003 International University Line La Jolla, CA 39 55
    • (2003) Methods and Results in Crystallization of Membrane Proteins , pp. 39-55
    • Landau, E.M.1
  • 23
    • 33745321115 scopus 로고    scopus 로고
    • The physics of protein crystallization
    • H. Ehrenreich F. Spaepen Academic Press New York
    • P.G. Vekilov, and A.A. Chernov The physics of protein crystallization H. Ehrenreich F. Spaepen Solid State Physics vol. 57 2002 Academic Press New York 1 147
    • (2002) Solid State Physics , vol.57 , pp. 1-147
    • Vekilov, P.G.1    Chernov, A.A.2
  • 25
    • 0035979794 scopus 로고    scopus 로고
    • Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases
    • P. Nollert, H. Qiu, M. Caffrey, J.P. Rosenbusch, and E.M. Landau Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases FEBS Letters 504 2001 179 186
    • (2001) FEBS Letters , vol.504 , pp. 179-186
    • Nollert, P.1    Qiu, H.2    Caffrey, M.3    Rosenbusch, J.P.4    Landau, E.M.5
  • 26
    • 5544258281 scopus 로고    scopus 로고
    • Crystallization of a polar protein and small molecules from the aqueous compartments of lipidic cubic phases
    • E.M. Landau, G. Rummel, S.W. Cowan-Jacob, and J.P. Rosenbusch Crystallization of a polar protein and small molecules from the aqueous compartments of lipidic cubic phases J. Phys. Chem. B 101 1997 1935 1946
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1935-1946
    • Landau, E.M.1    Rummel, G.2    Cowan-Jacob, S.W.3    Rosenbusch, J.P.4
  • 27
    • 0000067621 scopus 로고
    • The growth of crystals and equilibrium structure of their surfaces
    • W.K. Burton, N. Cabrera, and F.C. Frank The growth of crystals and equilibrium structure of their surfaces Philos. Trans. Roy. Soc. ser. A 243 1951 299 360
    • (1951) Philos. Trans. Roy. Soc. Ser. a , vol.243 , pp. 299-360
    • Burton, W.K.1    Cabrera, N.2    Frank, F.C.3
  • 28
    • 0344668506 scopus 로고
    • Elementary processes of protein crystal growth
    • H. Komatsu Pergamon Oxford
    • P.G. Vekilov Elementary processes of protein crystal growth H. Komatsu Studies and Concepts in Crystal Growth 1993 Pergamon Oxford 25 49
    • (1993) Studies and Concepts in Crystal Growth , pp. 25-49
    • Vekilov, P.G.1
  • 29
    • 0030084577 scopus 로고    scopus 로고
    • Dependence of lysozyme growth kinetics on step sources and impurities
    • P.G. Vekilov, and F. Rosenberger Dependence of lysozyme growth kinetics on step sources and impurities J. Crystal Growth 158 1996 540 551
    • (1996) J. Crystal Growth , vol.158 , pp. 540-551
    • Vekilov, P.G.1    Rosenberger, F.2
  • 30
    • 0031191579 scopus 로고    scopus 로고
    • An in-situ AFM investigation of canavalin crystallization kinetics
    • T.A. Land, J.J. DeYoreo, and J.D. Lee An in-situ AFM investigation of canavalin crystallization kinetics Surf. Sci. 384 1997 136 155
    • (1997) Surf. Sci. , vol.384 , pp. 136-155
    • Land, T.A.1    Deyoreo, J.J.2    Lee, J.D.3
  • 32
    • 0141757424 scopus 로고    scopus 로고
    • Capillarity effects on the crystallization kinetics: Insulin
    • I. Reviakine, D.K. Georgiou, and P.G. Vekilov Capillarity effects on the crystallization kinetics: insulin J. Am. Chem. Soc. 125 2003 11684 11693
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11684-11693
    • Reviakine, I.1    Georgiou, D.K.2    Vekilov, P.G.3
  • 33
    • 0006047430 scopus 로고
    • Über die Thomson-Gibbs'sche Gleichung bei Kristallen
    • R. Kaischew, and I.N. Stranski Über die Thomson-Gibbs'sche Gleichung bei Kristallen Z. Phys. Chem. B 35 1937 427 432
    • (1937) Z. Phys. Chem. B , vol.35 , pp. 427-432
    • Kaischew, R.1    Stranski, I.N.2
  • 34
    • 0029645277 scopus 로고
    • The science of macromolecular crystallization
    • A. McPherson, A.J. Malkin, and Y.G. Kuznetsov The science of macromolecular crystallization Structure 3 1995 759 768
    • (1995) Structure , vol.3 , pp. 759-768
    • McPherson, A.1    Malkin, A.J.2    Kuznetsov, Y.G.3
  • 36
    • 42749098588 scopus 로고    scopus 로고
    • Dissipating step bunches during crystallization under transport control
    • H. Lin, S.-T. Yau, and P.G. Vekilov Dissipating step bunches during crystallization under transport control Phys. Rev. E 67 2003 0031606
    • (2003) Phys. Rev. e , vol.67 , pp. 0031606
    • Lin, H.1    Yau, S.-T.2    Vekilov, P.G.3
  • 37
    • 0033513796 scopus 로고    scopus 로고
    • AFM stuides of the nucleation and growth mechanisms of macromolecular crystals
    • Y.G. Kuznetsov, A.J. Malkin, and A. McPherson AFM stuides of the nucleation and growth mechanisms of macromolecular crystals J. Crystal Growth 196 1999 489 502
    • (1999) J. Crystal Growth , vol.196 , pp. 489-502
    • Kuznetsov, Y.G.1    Malkin, A.J.2    McPherson, A.3
  • 39
    • 0033689048 scopus 로고    scopus 로고
    • Dynamics of layer growth in protein crystallization
    • P.G. Vekilov, and J.I.D. Alexander Dynamics of layer growth in protein crystallization Chem. Rev. 100 2000 2061 2089
    • (2000) Chem. Rev. , vol.100 , pp. 2061-2089
    • Vekilov, P.G.1    Alexander, J.I.D.2
  • 40
    • 0344234384 scopus 로고    scopus 로고
    • Molecular mechanisms of defect formation
    • C.W. Carter Jr R.M. Sweet Academic Press San Diego
    • P.G. Vekilov Molecular mechanisms of defect formation C.W. Carter Jr R.M. Sweet Methods in Enzymology vol. 368 2003 Academic Press San Diego 170 188 part C
    • (2003) Methods in Enzymology , vol.368 , pp. 170-188
    • Vekilov, P.G.1
  • 41
    • 0037391987 scopus 로고    scopus 로고
    • Protein crystals and their growth
    • A.A. Chernov Protein crystals and their growth J. Struct. Biol. 142 2003 3 21
    • (2003) J. Struct. Biol. , vol.142 , pp. 3-21
    • Chernov, A.A.1
  • 43
    • 0029734665 scopus 로고    scopus 로고
    • Biological atomic force microscopy: What is achieved and what is needed
    • Z. Shao, J. Mou, D.M. Czjkowsky, J. Yang, and J.Y. Yuan Biological atomic force microscopy: what is achieved and what is needed Advan. Phys. 45 1996 1 86
    • (1996) Advan. Phys. , vol.45 , pp. 1-86
    • Shao, Z.1    Mou, J.2    Czjkowsky, D.M.3    Yang, J.4    Yuan, J.Y.5
  • 44
    • 0033593012 scopus 로고    scopus 로고
    • Varieties of imaging with scanning probe microscopes
    • H.G. Hansma Varieties of imaging with scanning probe microscopes Proc. Natl Acad. Sci. USA 96 1999 14678 14680
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14678-14680
    • Hansma, H.G.1
  • 45
    • 0343777458 scopus 로고    scopus 로고
    • Observing single biomolecules at work with the atomic force microscope
    • A. Engel, and D.J. Müller Observing single biomolecules at work with the atomic force microscope Nature Struct. Biol. 7 2000 715 718
    • (2000) Nature Struct. Biol. , vol.7 , pp. 715-718
    • Engel, A.1    Müller, D.J.2
  • 46
    • 0034601474 scopus 로고    scopus 로고
    • Quasi-planar nucleus structure in apoferritin crystallisation
    • S.-T. Yau, and P.G. Vekilov Quasi-planar nucleus structure in apoferritin crystallisation Nature 406 2000 494 497
    • (2000) Nature , vol.406 , pp. 494-497
    • Yau, S.-T.1    Vekilov, P.G.2
  • 47
    • 2942602100 scopus 로고    scopus 로고
    • Scanning probe evolution in biology
    • J.K.H. Hörber, and M.J. Miles Scanning probe evolution in biology Science 302 2003 1002 1005
    • (2003) Science , vol.302 , pp. 1002-1005
    • Hörber, J.K.H.1    Miles, M.J.2
  • 48
    • 0027641096 scopus 로고
    • In situ studies of protein crystal growth by atomic force microscopy
    • S.D. Durbin, W.E. Carson, and M.T. Saros In situ studies of protein crystal growth by atomic force microscopy J. Phys. D 26 1993 B128 B132
    • (1993) J. Phys. D , vol.26
    • Durbin, S.D.1    Carson, W.E.2    Saros, M.T.3
  • 49
    • 4243657702 scopus 로고    scopus 로고
    • Molecular mechanisms of crystallization and defect formation
    • S.-T. Yau, B.R. Thomas, and P.G. Vekilov Molecular mechanisms of crystallization and defect formation Phys. Rev. Letters 85 2000 353 356
    • (2000) Phys. Rev. Letters , vol.85 , pp. 353-356
    • Yau, S.-T.1    Thomas, B.R.2    Vekilov, P.G.3
  • 50
    • 85003353363 scopus 로고    scopus 로고
    • Stable equidistant step trains during crystallization of insulin
    • O. Gliko, I. Reviakine, and P.G. Vekilov Stable equidistant step trains during crystallization of insulin Phys. Rev. Letters 2003 90
    • (2003) Phys. Rev. Letters , pp. 90
    • Gliko, O.1    Reviakine, I.2    Vekilov, P.G.3
  • 51
    • 6344228842 scopus 로고    scopus 로고
    • Microscopic, mesoscopic, and macroscopic lengthscales in the kinetics of phase transformations with proteins
    • J.J. De Yoreo X.Y. Lui Kluwer Press New York
    • P.G. Vekilov Microscopic, mesoscopic, and macroscopic lengthscales in the kinetics of phase transformations with proteins J.J. De Yoreo X.Y. Lui Nanoscale Structure and Assembly at Solid-Fluid Interfaces 2004 Kluwer Press New York 145 200
    • (2004) Nanoscale Structure and Assembly at Solid-Fluid Interfaces , pp. 145-200
    • Vekilov, P.G.1
  • 52
    • 0026713828 scopus 로고
    • Atomic force microscopy of 3-dimensional membrane-protein crystals - Ca-ATPase of sarcoplasmic-reticulum
    • J.J. Lacapere, D.L. Stokes, and D. Chatenay Atomic force microscopy of 3-dimensional membrane-protein crystals - Ca-ATPase of sarcoplasmic-reticulum Biophys. J. 63 1992 303 308
    • (1992) Biophys. J. , vol.63 , pp. 303-308
    • Lacapere, J.J.1    Stokes, D.L.2    Chatenay, D.3
  • 53
    • 4344664565 scopus 로고    scopus 로고
    • Probing of crystal interfaces and the structures and dynamic properties of large macromolecular ensembles with in situ atomic force microscopy
    • J.J. De Yoreo X.Y. Lui Plenum/Kluwer Academic New York
    • A.J. Malkin, and A. McPherson Probing of crystal interfaces and the structures and dynamic properties of large macromolecular ensembles with in situ atomic force microscopy J.J. De Yoreo X.Y. Lui From Fluid-Solid Interfaces to Nanostructural Engineering vol. 2 2004 Plenum/Kluwer Academic New York 201 238
    • (2004) From Fluid-Solid Interfaces to Nanostructural Engineering , vol.2 , pp. 201-238
    • Malkin, A.J.1    McPherson, A.2
  • 54
    • 0345045330 scopus 로고    scopus 로고
    • Anomalous lateral size measurements by atomic force microscopy in a fluid cell
    • G.A. Neff, D.E. Gragson, D.A. Shon, and S.M. Baker Anomalous lateral size measurements by atomic force microscopy in a fluid cell Langmuir 15 1999 2999 3002
    • (1999) Langmuir , vol.15 , pp. 2999-3002
    • Neff, G.A.1    Gragson, D.E.2    Shon, D.A.3    Baker, S.M.4
  • 55
    • 0031880366 scopus 로고    scopus 로고
    • Growth of protein 2-d crystals on supported planar lipid bilayers imaged in situ by AFM
    • I. Reviakine, W. Bergsma-Schutter, and A. Brisson Growth of protein 2-d crystals on supported planar lipid bilayers imaged in situ by AFM J. Struct. Biol. 121 1998 356 362
    • (1998) J. Struct. Biol. , vol.121 , pp. 356-362
    • Reviakine, I.1    Bergsma-Schutter, W.2    Brisson, A.3
  • 56
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous-solutions at subnanometer resolution by atomic-force microscopy
    • D.J. Muller, F.A. Schabert, G. Buldt, and A. Engel Imaging purple membranes in aqueous-solutions at subnanometer resolution by atomic-force microscopy Biophys. J. 68 1995 1681 1686
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Muller, D.J.1    Schabert, F.A.2    Buldt, G.3    Engel, A.4
  • 57
    • 0037417873 scopus 로고    scopus 로고
    • Diffusion-limited kinetics of the solution-solid phase transition of molecular substances
    • D.N. Petsev, K. Chen, O. Gliko, and P.G. Vekilov Diffusion-limited kinetics of the solution-solid phase transition of molecular substances Proc. Natl Acad. Sci. USA 100 2003 792 796
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 792-796
    • Petsev, D.N.1    Chen, K.2    Gliko, O.3    Vekilov, P.G.4
  • 60
    • 0033513872 scopus 로고    scopus 로고
    • Estimates of internal stress and related mosaicity in solution grown crystals: Proteins
    • A.A. Chernov Estimates of internal stress and related mosaicity in solution grown crystals: proteins J. Crystal Growth 196 1999 524 534
    • (1999) J. Crystal Growth , vol.196 , pp. 524-534
    • Chernov, A.A.1
  • 61
    • 0035371520 scopus 로고    scopus 로고
    • Molecular mechanisms of microheterogeneity-induced defect formation in ferritin crystallization
    • S.-T. Yau, B.R. Thomas, O. Galkin, O. Gliko, and P.G. Vekilov Molecular mechanisms of microheterogeneity-induced defect formation in ferritin crystallization Proteins: Struct. Funct. Genet. 43 2001 343 352
    • (2001) Proteins: Struct. Funct. Genet. , vol.43 , pp. 343-352
    • Yau, S.-T.1    Thomas, B.R.2    Galkin, O.3    Gliko, O.4    Vekilov, P.G.5
  • 62
    • 0001370636 scopus 로고
    • Thermodynamic stability conditions for the occurrence of hollow cores caused by stress of line and planar defects
    • B. Van den Hoek, J.P. Van der Eerden, and P. Bennema Thermodynamic stability conditions for the occurrence of hollow cores caused by stress of line and planar defects J. Crystal Growth 56 1982 621 632
    • (1982) J. Crystal Growth , vol.56 , pp. 621-632
    • Van Den Hoek, B.1    Van Der Eerden, J.P.2    Bennema, P.3
  • 63
    • 0000201014 scopus 로고    scopus 로고
    • Nonlinear response of layer growth dynamics in the mixed kinetics-bulk transport regime
    • P.G. Vekilov, J.I.D. Alexander, and F. Rosenberger Nonlinear response of layer growth dynamics in the mixed kinetics-bulk transport regime Phys. Rev. E 54 1996 6650 6660
    • (1996) Phys. Rev. e , vol.54 , pp. 6650-6660
    • Vekilov, P.G.1    Alexander, J.I.D.2    Rosenberger, F.3
  • 64
    • 0025096943 scopus 로고
    • Large-scale preparation of homogeneous bacteriorhodopsin
    • B. Lorber, and L.J. Delucas Large-scale preparation of homogeneous bacteriorhodopsin FEBS Letters 261 1990 14 18
    • (1990) FEBS Letters , vol.261 , pp. 14-18
    • Lorber, B.1    Delucas, L.J.2
  • 66
    • 0032414367 scopus 로고    scopus 로고
    • Enzymic release of crystals from lipidic cubic phases
    • P. Nollert, and E.M. Landau Enzymic release of crystals from lipidic cubic phases Biochem. Soc. Trans. 26 1998 709 713
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 709-713
    • Nollert, P.1    Landau, E.M.2
  • 67
    • 0031194571 scopus 로고    scopus 로고
    • Adsorption of biological molecules to a solid support for scanning probe microscopy
    • D.J. Muller, M. Amrein, and A. Engel Adsorption of biological molecules to a solid support for scanning probe microscopy J. Struct. Biol. 119 1997 172 188
    • (1997) J. Struct. Biol. , vol.119 , pp. 172-188
    • Muller, D.J.1    Amrein, M.2    Engel, A.3
  • 68
    • 0027591723 scopus 로고
    • Laser Michelson interferometry investigation of protein crystal growth
    • P.G. Vekilov, M. Ataka, and T. Katsura Laser Michelson interferometry investigation of protein crystal growth J. Crystal Growth 130 1993 317 320
    • (1993) J. Crystal Growth , vol.130 , pp. 317-320
    • Vekilov, P.G.1    Ataka, M.2    Katsura, T.3
  • 69
    • 0029132454 scopus 로고
    • Growth processes of protein crystals revealed by laser Michelson interferometry investigation
    • P.G. Vekilov, M. Ataka, and T. Katsura Growth processes of protein crystals revealed by laser Michelson interferometry investigation Acta Crystallog. sect. D 51 1995 207 219
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 207-219
    • Vekilov, P.G.1    Ataka, M.2    Katsura, T.3


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