메뉴 건너뛰기




Volumn 1270, Issue , 2010, Pages 60-77

Nucleation of crystals in solution

Author keywords

classical nucleation theory; dense liquid; phase diagram; spinodal; two step nucleation mechanism

Indexed keywords


EID: 77955595706     PISSN: 0094243X     EISSN: 15517616     Source Type: Conference Proceeding    
DOI: 10.1063/1.3476239     Document Type: Conference Paper
Times cited : (10)

References (97)
  • 4
    • 0030565978 scopus 로고    scopus 로고
    • Protein crystal growth in microgravity review of large scale temperature induction method
    • M. L. Long, J. B. Bishop, T. L. Nagabhushan, et al., Protein crystal growth in microgravity review of large scale temperature induction method. J. Crystal Growth 168, 233 (1996).
    • (1996) J. Crystal Growth , vol.168 , pp. 233
    • Long, M.L.1    Bishop, J.B.2    Nagabhushan, T.L.3
  • 5
    • 0024337499 scopus 로고
    • New crystal form of recombinant murine interferon-β
    • S. Matsuda, T. Senda, S. Itoh, et al., New crystal form of recombinant murine interferon-β. J. Biol. Chem 264, 13381 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 13381
    • Matsuda, S.1    Senda, T.2    Itoh, S.3
  • 6
    • 0007229114 scopus 로고
    • edited by C. C. Richardson, P. D. Boyer, I. B. Dawid and A. Meister Annual Reviews, Palo Alto
    • S. Peseta, J. A. Langer, K. C. Zoon, et al., in Annual Review of Biochemistry, edited by C. C. Richardson, P. D. Boyer, I. B. Dawid and A. Meister (Annual Reviews, Palo Alto, 1989), Vol. 56, p. 727.
    • (1989) Annual Review of Biochemistry , vol.56 , pp. 727
    • Peseta, S.1    Langer, J.A.2    Zoon, K.C.3
  • 7
    • 0014149925 scopus 로고
    • Pathogenesis of hemolytic anemia in homozygous hemoglobin C disease
    • S. Charache, C. L. Conley, D. F. Waugh, et al., Pathogenesis of hemolytic anemia in homozygous hemoglobin C disease. J Clin Invest 46, 1795 (1967).
    • (1967) J Clin Invest , vol.46 , pp. 1795
    • Charache, S.1    Conley, C.L.2    Waugh, D.F.3
  • 8
    • 0021996069 scopus 로고
    • Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients
    • R. E. Hirsch, C. Raventos-Suarez, J. A. Olson, et al., Ligand state of intraerythrocytic circulating HbC crystals in homozygote CC patients. Blood 66, 775 (1985).
    • (1985) Blood , vol.66 , pp. 775
    • Hirsch, R.E.1    Raventos-Suarez, C.2    Olson, J.A.3
  • 9
    • 0025276708 scopus 로고
    • edited by C. B. Anfinsen, J. T. Edsal, F. M. Richards and D. S. Eisenberg Academic Press, San Diego
    • W. A. Eaton and J. Hofrichter, in Advances in protein chemistry, edited by C. B. Anfinsen, J. T. Edsal, F. M. Richards and D. S. Eisenberg (Academic Press, San Diego, 1990), Vol. 40, p. 63.
    • (1990) Advances in Protein Chemistry , vol.40 , pp. 63
    • Eaton, W.A.1    Hofrichter, J.2
  • 10
    • 34848813177 scopus 로고    scopus 로고
    • Sickle-cell haemoglobin polymerisation: Is it the primary pathogenic event of sickle-cell anaemia?
    • P. Vekilov, Sickle-cell haemoglobin polymerisation: is it the primary pathogenic event of sickle-cell anaemia? Brit. J. Haematol. 139, 173 (2007).
    • (2007) Brit. J. Haematol. , vol.139 , pp. 173
    • Vekilov, P.1
  • 12
    • 0035824869 scopus 로고    scopus 로고
    • Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin
    • N. Asherie, J. Pande, A. Pande, et al., Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin. J Mol Biol 314, 663 (2001).
    • (2001) J Mol Biol , vol.314 , pp. 663
    • Asherie, N.1    Pande, J.2    Pande, A.3
  • 16
    • 34547894189 scopus 로고    scopus 로고
    • Three frontiers in the thermodynamics of protein solutions
    • J. Prausnitz and L. Foose, Three frontiers in the thermodynamics of protein solutions. Pure and Applied Chemistry 79, 1435 (2007).
    • (2007) Pure and Applied Chemistry , vol.79 , pp. 1435
    • Prausnitz, J.1    Foose, L.2
  • 18
    • 0035501930 scopus 로고    scopus 로고
    • Temperature-independent Solubility and Interactions between Apoferritin Monomers and Dimers in Solution
    • D. N. Petsev, B. R. Thomas, S.-T. Yau, et al., Temperature-independent Solubility and Interactions between Apoferritin Monomers and Dimers in Solution. J. Crystal Growth 232, 21 (2001).
    • (2001) J. Crystal Growth , vol.232 , pp. 21
    • Petsev, D.N.1    Thomas, B.R.2    Yau, S.-T.3
  • 20
    • 0000063775 scopus 로고
    • On the equilibrium of heterogeneous substances
    • J. W. Gibbs, On the equilibrium of heterogeneous substances. Trans. Connect. Acad. Sci. 3, 108 (1876).
    • (1876) Trans. Connect. Acad. Sci. , vol.3 , pp. 108
    • Gibbs, J.W.1
  • 21
    • 0000063775 scopus 로고
    • On the equilibrium of heterogeneous substances
    • J. W. Gibbs, On the equilibrium of heterogeneous substances. Trans. Connect. Acad. Sci. 16, 343 (1878).
    • (1878) Trans. Connect. Acad. Sci. , vol.16 , pp. 343
    • Gibbs, J.W.1
  • 23
    • 0001615603 scopus 로고
    • edited by D. T. J. Hurle Elsevier, Amsterdam
    • B. Mutaftschiev, in Handbook of crystal growth, edited by D. T. J. Hurle (Elsevier, Amsterdam, 1993), Vol. I, p. 189.
    • (1993) Handbook of Crystal Growth , vol.1 , pp. 189
    • Mutaftschiev, B.1
  • 24
    • 0030498908 scopus 로고    scopus 로고
    • Repartitioning of NaCl and protein impurities in lysozyme crystallization
    • P. G. Vekilov, L. A. Monaco, B. R. Thomas, et al., Repartitioning of NaCl and protein impurities in lysozyme crystallization. Acta Crystallogr. Section D 52, 785 (1996).
    • (1996) Acta Crystallogr. Section D , vol.52 , pp. 785
    • Vekilov, P.G.1    Monaco, L.A.2    Thomas, B.R.3
  • 25
    • 36849108755 scopus 로고
    • On the Statistical Mechanics of Nucleation Theory
    • J. Lothe and G. M. Pound, On the Statistical Mechanics of Nucleation Theory. The Journal of Chemical Physics 45, 630 (1966).
    • (1966) The Journal of Chemical Physics , vol.45 , pp. 630
    • Lothe, J.1    Pound, G.M.2
  • 26
    • 0026053018 scopus 로고
    • Binary liquid phase separation of lens proteins solutions
    • M. L. Broide, C. R. Berland, J. Pande, et al., Binary liquid phase separation of lens proteins solutions. Proc. Natl. Acad. Sci. USA 88, 5660 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5660
    • Broide, M.L.1    Berland, C.R.2    Pande, J.3
  • 27
    • 0031559476 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization
    • M. Muschol and F. Rosenberger, Liquid-liquid phase separation in supersaturated lysozyme solutions and associated precipitate formation/crystallization. J. Chem. Phys. 107, 1953 (1997).
    • (1997) J. Chem. Phys. , vol.107 , pp. 1953
    • Muschol, M.1    Rosenberger, F.2
  • 28
    • 0344408851 scopus 로고    scopus 로고
    • Thermodynamic functions of concentrated protein solutions from phase equilibria
    • D. N. Petsev, X. Wu, O. Galkin, et al., Thermodynamic functions of concentrated protein solutions from phase equilibria. J. Phys. Chem. B 107, 3921 (2003).
    • (2003) J. Phys. Chem. B , vol.107 , pp. 3921
    • Petsev, D.N.1    Wu, X.2    Galkin, O.3
  • 29
    • 0037459494 scopus 로고    scopus 로고
    • Solution crystallization via a submerged liquid-liquid phase boundary: Oiling out
    • P. E. Bonnett, K. J. Carpenter, S. Dawson, et al., Solution crystallization via a submerged liquid-liquid phase boundary: oiling out. Chem. Commun., 698 (2003).
    • (2003) Chem. Commun. , vol.698
    • Bonnett, P.E.1    Carpenter, K.J.2    Dawson, S.3
  • 30
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • P. R. ten Wolde and D. Frenkel, Enhancement of protein crystal nucleation by critical density fluctuations. Science 277, 1975 (1997).
    • (1997) Science , vol.277 , pp. 1975
    • Ten Wolde, P.R.1    Frenkel, D.2
  • 31
    • 0001052492 scopus 로고    scopus 로고
    • Crystal nucleation in the presence of a metastable critical point
    • V. Talanquer and D. W. Oxtoby, Crystal nucleation in the presence of a metastable critical point. J. Chem. Phys. 109, 223 (1998).
    • (1998) J. Chem. Phys. , vol.109 , pp. 223
    • Talanquer, V.1    Oxtoby, D.W.2
  • 32
    • 0037961013 scopus 로고    scopus 로고
    • Metastable states and the kinetics of colloid phase separation
    • K. G. Soga, J. M. Melrose, and R. C. Ball, Metastable states and the kinetics of colloid phase separation. J. Chem. Phys. 110, 2280 (1999).
    • (1999) J. Chem. Phys. , vol.110 , pp. 2280
    • Soga, K.G.1    Melrose, J.M.2    Ball, R.C.3
  • 33
    • 0023430928 scopus 로고
    • Binary liquid phase separation and critical phenomena in a protein water solution
    • J. A. Thomson, P. Schurtenberger, G. M. Thurston, et al., Binary liquid phase separation and critical phenomena in a protein water solution. Proc. Natl. Acad. Sci. USA 84, 7079 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7079
    • Thomson, J.A.1    Schurtenberger, P.2    Thurston, G.M.3
  • 35
    • 0037153184 scopus 로고    scopus 로고
    • Crystals in a flash
    • D. W. Oxtoby, Crystals in a flash. Nature 420, 277 (2002).
    • (2002) Nature , vol.420 , pp. 277
    • Oxtoby, D.W.1
  • 36
    • 4143146536 scopus 로고    scopus 로고
    • Dense liquid precursor for the nucleation of ordered solid phases from solution
    • P. G. Vekilov, Dense liquid precursor for the nucleation of ordered solid phases from solution. Crystal Growth and Design 4, 671 (2004).
    • (2004) Crystal Growth and Design , vol.4 , pp. 671
    • Vekilov, P.G.1
  • 37
    • 0034612274 scopus 로고    scopus 로고
    • Control of protein crystal nucleation around the metastable liquid-liquid phase boundary
    • O. Galkin and P. G. Vekilov, Control of protein crystal nucleation around the metastable liquid-liquid phase boundary. Proc. Natl. Acad. Sci. USA 97, 6277 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6277
    • Galkin, O.1    Vekilov, P.G.2
  • 38
    • 0037171856 scopus 로고    scopus 로고
    • Insights into phase transition kinetics from colloid science
    • V. J. Anderson and H. N. W. Lekkerkerker, Insights into phase transition kinetics from colloid science. Nature 416, 811 (2002).
    • (2002) Nature , vol.416 , pp. 811
    • Anderson, V.J.1    Lekkerkerker, H.N.W.2
  • 39
    • 0000540719 scopus 로고    scopus 로고
    • Direct determination of the nucleation rate of protein crystals
    • O. Galkin and P. G. Vekilov, Direct determination of the nucleation rate of protein crystals. J. Phys. Chem. 103, 10965 (1999).
    • (1999) J. Phys. Chem. , vol.103 , pp. 10965
    • Galkin, O.1    Vekilov, P.G.2
  • 40
    • 0037470883 scopus 로고    scopus 로고
    • On the methods of determination of homogeneous nucleation rates of protein crystals
    • P. G. Vekilov and O. Galkin, On the methods of determination of homogeneous nucleation rates of protein crystals. Colloids and Surfaces A 215, 125 (2003).
    • (2003) Colloids and Surfaces A , vol.215 , pp. 125
    • Vekilov, P.G.1    Galkin, O.2
  • 41
    • 36749114484 scopus 로고
    • On the relation between nucleation work, nucleus size, and nucleation rate
    • D. Kashchiev, On the relation between nucleation work, nucleus size, and nucleation rate. The Journal of Chemical Physics 76, 5098 (1982).
    • (1982) The Journal of Chemical Physics , vol.76 , pp. 5098
    • Kashchiev, D.1
  • 42
    • 0001511066 scopus 로고
    • A general relation between the nucleation work and the size of the nucleus in multicomponent nucleation
    • D. W. Oxtoby and D. Kashchiev, A general relation between the nucleation work and the size of the nucleus in multicomponent nucleation. The Journal of Chemical Physics 100, 7665 (1994).
    • (1994) The Journal of Chemical Physics , vol.100 , pp. 7665
    • Oxtoby, D.W.1    Kashchiev, D.2
  • 45
    • 33746012315 scopus 로고
    • Free energy of a nonuniform system. I. Interfacial free energy
    • J. W. Cahn and J. E. Hilliard, Free energy of a nonuniform system. I. Interfacial free energy. The Journal of Chemical Physics 28, 258 (1958).
    • (1958) The Journal of Chemical Physics , vol.28 , pp. 258
    • Cahn, J.W.1    Hilliard, J.E.2
  • 48
    • 18744399040 scopus 로고    scopus 로고
    • Nucleation of ordered solid phases of protein via a disordered high-density state: Phenomenological approach
    • W. Pan, A. B. Kolomeisky, and P. G. Vekilov, Nucleation of ordered solid phases of protein via a disordered high-density state: Phenomenological approach. J. Chem. Phys. 122, 174905 (2005).
    • (2005) J. Chem. Phys. , vol.122 , pp. 174905
    • Pan, W.1    Kolomeisky, A.B.2    Vekilov, P.G.3
  • 50
    • 61549091507 scopus 로고    scopus 로고
    • Comparison of Different Experimental Techniques for the Measurement of Crystal Growth Kinetics†
    • A. E. S. Van Driessche, F. n. Otálora, G. Sazaki, et al., Comparison of Different Experimental Techniques for the Measurement of Crystal Growth Kinetics†. Crystal Growth & Design 8, 4316 (2008).
    • (2008) Crystal Growth & Design , vol.8 , pp. 4316
    • Van Driessche, A.E.S.1    Otálora, F.N.2    Sazaki, G.3
  • 51
    • 0033513864 scopus 로고    scopus 로고
    • In situ atomic force microscopy studies of surface morphology, growth kinetics, defect structure and dissolution in macromolecular crystallization
    • A. J. Malkin, Y. G. Kuznetsov, and A. McPherson, In situ atomic force microscopy studies of surface morphology, growth kinetics, defect structure and dissolution in macromolecular crystallization. J. Crystal Growth 196, 471 (1999).
    • (1999) J. Crystal Growth , vol.196 , pp. 471
    • Malkin, A.J.1    Kuznetsov, Y.G.2    McPherson, A.3
  • 52
    • 0000015259 scopus 로고    scopus 로고
    • Effects of convective solute and impurity transport on protein crystal growth
    • P. G. Vekilov, B. R. Thomas, and F. Rosenberger, Effects of convective solute and impurity transport on protein crystal growth. J. Phys. Chem. B 102, 5208 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 5208
    • Vekilov, P.G.1    Thomas, B.R.2    Rosenberger, F.3
  • 53
    • 0003056570 scopus 로고
    • Theory of new phase formation: Cavitation
    • Y. B. Zel'dovich, Theory of new phase formation: Cavitation. Acta Physicochimica URSS 18, 1 (1943).
    • (1943) Acta Physicochimica URSS , vol.18 , pp. 1
    • Zel'Dovich, Y.B.1
  • 54
    • 0002190262 scopus 로고
    • edited by J. P. v. d. Eerden and O. S. L. Bruinsma Kluwer Academic Publishers
    • D. Kashchiev, in Science and technology of crystal growth, edited by J. P. v. d. Eerden and O. S. L. Bruinsma (Kluwer Academic Publishers, 1995), p. 53.
    • (1995) Science and Technology of Crystal Growth , pp. 53
    • Kashchiev, D.1
  • 56
    • 0034639421 scopus 로고    scopus 로고
    • Are nucleation kinetics of protein crystals similar to those of liquid droplets?
    • O. Galkin and P. G. Vekilov, Are nucleation kinetics of protein crystals similar to those of liquid droplets? J. Amer. Chem. Soc. 122, 156 (2000).
    • (2000) J. Amer. Chem. Soc. , vol.122 , pp. 156
    • Galkin, O.1    Vekilov, P.G.2
  • 57
    • 8344242992 scopus 로고    scopus 로고
    • Smooth transition from metastability to instability in phase separating protein solutions
    • M. Shah, O. Galkin, and P. G. Vekilov, Smooth transition from metastability to instability in phase separating protein solutions. J. Chem. Phys. 121, 7505 (2004).
    • (2004) J. Chem. Phys. , vol.121 , pp. 7505
    • Shah, M.1    Galkin, O.2    Vekilov, P.G.3
  • 58
    • 0002268479 scopus 로고
    • Preliminary x-ray data for some crystaline forms of β-lactoglobulin and hen egg-white lysozyme
    • L. K. Steinrauf, Preliminary x-ray data for some crystaline forms of β-lactoglobulin and hen egg-white lysozyme. Acta Crystallogr. 12, 77 (1959).
    • (1959) Acta Crystallogr , vol.12 , pp. 77
    • Steinrauf, L.K.1
  • 59
    • 0027560477 scopus 로고
    • Light scattering investigations of protein and virus crystal growth: Ferritin, apoferritin and satellite tobacco mosaic virus
    • A. J. Malkin and A. McPherson, Light scattering investigations of protein and virus crystal growth: ferritin, apoferritin and satellite tobacco mosaic virus. J. Crystal Growth 128, 1232 (1993).
    • (1993) J. Crystal Growth , vol.128 , pp. 1232
    • Malkin, A.J.1    McPherson, A.2
  • 60
    • 0000083867 scopus 로고
    • Light scattering investigation of the nucleation processes and kinetics of crystallization in macromolecular systems
    • A. J. Malkin and A. McPherson, Light scattering investigation of the nucleation processes and kinetics of crystallization in macromolecular systems. Acta Crystallogr. Section D 50, 385 (1994).
    • (1994) Acta Crystallogr. Section D , vol.50 , pp. 385
    • Malkin, A.J.1    McPherson, A.2
  • 61
    • 23844458001 scopus 로고    scopus 로고
    • Quantitative Imaging by Confocal Scanning Fluorescence Microscopy of Protein Crystallization via Liquid-Liquid Phase Separation
    • D. Vivares, E. Kaler, and A. Lenhoff, Quantitative Imaging by Confocal Scanning Fluorescence Microscopy of Protein Crystallization via Liquid-Liquid Phase Separation. Acta Crystallogr D Biol Crystallogr. 61, 819 (2005).
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 819
    • Vivares, D.1    Kaler, E.2    Lenhoff, A.3
  • 62
    • 0037172992 scopus 로고    scopus 로고
    • Liquid-liquid separation in solutions of normal and sickle cell hemoglobin
    • O. Galkin, K. Chen, R. L. Nagel, et al., Liquid-liquid separation in solutions of normal and sickle cell hemoglobin. Proc. Natl. Acad. Sci. USA 99, 8479 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8479
    • Galkin, O.1    Chen, K.2    Nagel, R.L.3
  • 63
    • 33846016196 scopus 로고    scopus 로고
    • Metastable mesoscopic clusters in solutions of sickle cell hemoglobin
    • W. Pan, O. Galkin, L. Filobelo, et al., Metastable mesoscopic clusters in solutions of sickle cell hemoglobin. Biophys. J. 92, 267 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 267
    • Pan, W.1    Galkin, O.2    Filobelo, L.3
  • 64
    • 77953148643 scopus 로고    scopus 로고
    • The origin of anomalous mesoscopic phases in protein solutions
    • in print
    • W. Pan, P. G. Vekilov, and V. Lubchenko, The origin of anomalous mesoscopic phases in protein solutions. J. Phys. Chem. B in print (2010).
    • (2010) J. Phys. Chem. B
    • Pan, W.1    Vekilov, P.G.2    Lubchenko, V.3
  • 65
    • 34147145913 scopus 로고    scopus 로고
    • Metastable liquid clusters in super- And undersaturated protein solutions
    • O. Gliko, W. Pan, P. Katsonis, et al., Metastable liquid clusters in super- and undersaturated protein solutions. J. Phys. Chem. B 111, 3106 (2007).
    • (2007) J. Phys. Chem. B , vol.111 , pp. 3106
    • Gliko, O.1    Pan, W.2    Katsonis, P.3
  • 66
    • 60549105262 scopus 로고    scopus 로고
    • Viscoelasticity in Homogeneous Protein Solutions
    • W. Pan, L. Filobelo, N. D. Q. Pham, et al., Viscoelasticity in Homogeneous Protein Solutions. Physical Review Letters 102, 058101 (2009).
    • (2009) Physical Review Letters , vol.102 , pp. 058101
    • Pan, W.1    Filobelo, L.2    Pham, N.D.Q.3
  • 67
    • 14944365598 scopus 로고    scopus 로고
    • A metastable prerequisite for the growth of lumazine synthase crystals
    • O. Gliko, N. Neumaier, W. Pan, et al., A metastable prerequisite for the growth of lumazine synthase crystals. J. Amer. Chem. Soc. 127, 3433 (2005).
    • (2005) J. Amer. Chem. Soc. , vol.127 , pp. 3433
    • Gliko, O.1    Neumaier, N.2    Pan, W.3
  • 68
    • 33846016337 scopus 로고
    • Excess Scattered-Light Intensity Fluctuations from Hemoglobin
    • E. E. Uzgiris and D. C. Golibersuch, Excess Scattered-Light Intensity Fluctuations from Hemoglobin. Physical Review Letters 32, 37 (1974).
    • (1974) Physical Review Letters , vol.32 , pp. 37
    • Uzgiris, E.E.1    Golibersuch, D.C.2
  • 69
    • 19244365097 scopus 로고    scopus 로고
    • Equilibrium Cluster Phases and Low-Density Arrested Disordered States: The Role of Short-Range Attraction and Long-Range Repulsion
    • F. Sciortino, S. Mossa, E. Zaccarelli, et al., Equilibrium Cluster Phases and Low-Density Arrested Disordered States: The Role of Short-Range Attraction and Long-Range Repulsion. Phys. Rev. Lett. 93, 055701 (2004).
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 055701
    • Sciortino, F.1    Mossa, S.2    Zaccarelli, E.3
  • 70
    • 0035969723 scopus 로고    scopus 로고
    • Anomalously Large Equilibrium Clusters of Colloids
    • J. Groenewold and W. K. Kegel, Anomalously Large Equilibrium Clusters of Colloids. J. Phys. Chem. B 105, 11702 (2001).
    • (2001) J. Phys. Chem. B , vol.105 , pp. 11702
    • Groenewold, J.1    Kegel, W.K.2
  • 72
    • 10044228437 scopus 로고    scopus 로고
    • Ground-State Clusters for Short-Range Attractive and Long-Range Repulsive Potentials
    • S. Mossa, F. Sciortino, P. Tartaglia, et al., Ground-State Clusters for Short-Range Attractive and Long-Range Repulsive Potentials. Langmuir 20, 10756 (2004).
    • (2004) Langmuir , vol.20 , pp. 10756
    • Mossa, S.1    Sciortino, F.2    Tartaglia, P.3
  • 73
    • 9644259209 scopus 로고    scopus 로고
    • Equilibrium cluster formation in concentrated protein solutions and colloids
    • A. Stradner, H. Sedgwick, F. Cardinaux, et al., Equilibrium cluster formation in concentrated protein solutions and colloids. Nature 432, 492 (2004).
    • (2004) Nature , vol.432 , pp. 492
    • Stradner, A.1    Sedgwick, H.2    Cardinaux, F.3
  • 74
    • 0037460238 scopus 로고    scopus 로고
    • Thermodynamically consistent description of the work to form a nucleus of any size
    • D. Kashchiev, Thermodynamically consistent description of the work to form a nucleus of any size. J. Chem. Phys. 118, 1837 (2003).
    • (2003) J. Chem. Phys. , vol.118 , pp. 1837
    • Kashchiev, D.1
  • 75
    • 0028483006 scopus 로고
    • Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrations
    • W. J. Fredericks, M. C. Hammonds, S. B. Howard , et al., Density, thermal expansivity, viscosity and refractive index of lysozyme solutions at crystal growth concentrations. J. Crystal Growth 141, 183 (1994).
    • (1994) J. Crystal Growth , vol.141 , pp. 183
    • Fredericks, W.J.1    Hammonds, M.C.2    Howard, S.B.3
  • 76
    • 22844433290 scopus 로고    scopus 로고
    • Spinodal for the solution-to-crystal phase transformation
    • L. F. Filobelo, O. Galkin, and P. G. Vekilov, Spinodal for the solution-to-crystal phase transformation. J. Chem. Phys. 123, 014904 (2005).
    • (2005) J. Chem. Phys. , vol.123 , pp. 014904
    • Filobelo, L.F.1    Galkin, O.2    Vekilov, P.G.3
  • 79
    • 0025628154 scopus 로고
    • Entropy production as the selection rule between different growth morphologies
    • A. Hill, Entropy production as the selection rule between different growth morphologies. Nature 348, 426 (1990).
    • (1990) Nature , vol.348 , pp. 426
    • Hill, A.1
  • 80
    • 0001417742 scopus 로고
    • edited by A. C. Zettlemoyer Marcel Dekker, New York
    • A. G. Walton, in Nucleation, edited by A. C. Zettlemoyer (Marcel Dekker, New York, 1969), p. 225.
    • (1969) Nucleation , pp. 225
    • Walton, A.G.1
  • 82
    • 0037192517 scopus 로고    scopus 로고
    • Crystal Engineering: From Structure to Function
    • M. D. Hollingsworth, Crystal Engineering: from Structure to Function. Science 295, 2410 (2002).
    • (2002) Science , vol.295 , pp. 2410
    • Hollingsworth, M.D.1
  • 83
    • 0041526781 scopus 로고    scopus 로고
    • Synthesis of Zeolite As Ordered Multicrystal Arrays
    • J. S. Lee, Y.-J. Lee, E. L. Tae, et al., Synthesis of Zeolite As Ordered Multicrystal Arrays. Science 301, 818 (2003).
    • (2003) Science , vol.301 , pp. 818
    • Lee, J.S.1    Lee, Y.-J.2    Tae, E.L.3
  • 84
    • 0024038328 scopus 로고
    • The use of heterogeneous and epitaxial nucleants to promote the growt of protein crystals
    • A. McPherson and P. Shlichta, The use of heterogeneous and epitaxial nucleants to promote the growt of protein crystals. J. Crystal Growth 90, 47 (1988).
    • (1988) J. Crystal Growth , vol.90 , pp. 47
    • McPherson, A.1    Shlichta, P.2
  • 85
    • 0028913772 scopus 로고
    • The mechanism of protein crystal growth from lipid layers
    • S. A. Hemming, A. Bochkarev, S. A. Darst, et al., The mechanism of protein crystal growth from lipid layers. J. Mol. Biol. 246, 308 (1995).
    • (1995) J. Mol. Biol. , vol.246 , pp. 308
    • Hemming, S.A.1    Bochkarev, A.2    Darst, S.A.3
  • 86
    • 4243283850 scopus 로고    scopus 로고
    • Polarization switching of crystal structure in the nonphotochemical light-induced nucleation of supersaturated aqueous glycine solutions
    • B. Garetz, J. Matic, and A. Myerson, Polarization switching of crystal structure in the nonphotochemical light-induced nucleation of supersaturated aqueous glycine solutions. Phys. Rev. Lett. 89, 175501 (2002).
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 175501
    • Garetz, B.1    Matic, J.2    Myerson, A.3
  • 87
    • 0035502093 scopus 로고    scopus 로고
    • The liquid protein phase in crystallization: A case study intact immunoglobins
    • Y. G. Kuznetsov, A. J. Malkin, and A. McPherson, The liquid protein phase in crystallization: a case study intact immunoglobins. J. Crystal Growth 232, 30 (2001).
    • (2001) J. Crystal Growth , vol.232 , pp. 30
    • Kuznetsov, Y.G.1    Malkin, A.J.2    McPherson, A.3
  • 88
    • 33751513333 scopus 로고    scopus 로고
    • The kinetics of nucleation and growth of sickle cell hemoglobin fibers
    • O. Galkin, R. L. Nagel, and P. G. Vekilov, The kinetics of nucleation and growth of sickle cell hemoglobin fibers. J. Mol. Biol. 365, 425 (2007).
    • (2007) J. Mol. Biol. , vol.365 , pp. 425
    • Galkin, O.1    Nagel, R.L.2    Vekilov, P.G.3
  • 89
    • 34547700385 scopus 로고    scopus 로고
    • Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers
    • O. Galkin, W. Pan, L. Filobelo, et al., Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers. Biophys. J. 92, 902 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 902
    • Galkin, O.1    Pan, W.2    Filobelo, L.3
  • 90
    • 18144382316 scopus 로고    scopus 로고
    • Strong dc Electric Field Applied to Supersaturated Aqueous Glycine Solution Induces Nucleation of the Polymorph
    • J. E. Aber, S. Arnold, and B. A. Garetz, Strong dc Electric Field Applied to Supersaturated Aqueous Glycine Solution Induces Nucleation of the Polymorph. Phys. Rev. Lett. 94, 145503 (2005).
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 145503
    • Aber, J.E.1    Arnold, S.2    Garetz, B.A.3
  • 91
    • 24744460497 scopus 로고    scopus 로고
    • Ionic colloidal crystals of oppositely charged particles
    • M. E. Leunissen, C. G. Christova, A.-P. Hynninen, et al., Ionic colloidal crystals of oppositely charged particles. Nature 437, 235 (2005).
    • (2005) Nature , vol.437 , pp. 235
    • Leunissen, M.E.1    Christova, C.G.2    Hynninen, A.-P.3
  • 92
    • 66049157786 scopus 로고    scopus 로고
    • Experimental Evidence for Two-Step Nucleation in Colloidal Crystallization
    • J. R. Savage and A. D. Dinsmore, Experimental Evidence for Two-Step Nucleation in Colloidal Crystallization. Physical Review Letters 102 (2009).
    • (2009) Physical Review Letters , vol.102
    • Savage, J.R.1    Dinsmore, A.D.2
  • 93
    • 57449090928 scopus 로고    scopus 로고
    • Biomimetic Model Systems for Investigating the Amorphous Precursor Pathway and Its Role in Biomineralization
    • L. B. Gower, Biomimetic Model Systems for Investigating the Amorphous Precursor Pathway and Its Role in Biomineralization. Chemical Reviews 108, 4551 (2008).
    • (2008) Chemical Reviews , vol.108 , pp. 4551
    • Gower, L.B.1
  • 94
    • 62449098439 scopus 로고    scopus 로고
    • The Initial Stages of Template-Controlled CaCO3 Formation Revealed by Cryo-TEM
    • E. M. Pouget, P. H. H. Bomans, J. Goos, et al., The Initial Stages of Template-Controlled CaCO3 Formation Revealed by Cryo-TEM. Science 323, 1455 (2009).
    • (2009) Science , vol.323 , pp. 1455
    • Pouget, E.M.1    Bomans, P.H.H.2    Goos, J.3
  • 95
    • 57849165523 scopus 로고    scopus 로고
    • Stable Prenucleation Calcium Carbonate Clusters
    • D. Gebauer, A. Volkel, and H. Colfen, Stable Prenucleation Calcium Carbonate Clusters. Science 322, 1819 (2008).
    • (2008) Science , vol.322 , pp. 1819
    • Gebauer, D.1    Volkel, A.2    Colfen, H.3
  • 96
    • 0026260016 scopus 로고
    • The solubility of the tetragonal form of hen egg white lysozyme from pH 4.0 to 5.4
    • E. Cacioppo and M. L. Pusey, The solubility of the tetragonal form of hen egg white lysozyme from pH 4.0 to 5.4. Journal of Crystal Growth 114, 286 (1991).
    • (1991) Journal of Crystal Growth , vol.114 , pp. 286
    • Cacioppo, E.1    Pusey, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.