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Volumn 14, Issue 5, 2004, Pages 577-583

Turning protein crystallisation from an art into a science

Author keywords

[No Author keywords available]

Indexed keywords

LIQUID PARAFFIN; SILICONE OIL;

EID: 4744359693     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.08.002     Document Type: Review
Times cited : (175)

References (44)
  • 1
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • T.L. Blundell, H. Jhotti, and C. Abell High-throughput crystallography for lead discovery in drug design Nat Rev Drug Discov 1 2002 45 54
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhotti, H.2    Abell, C.3
  • 2
    • 0000055252 scopus 로고
    • Growth kinetics of tetragonal lysozyme crystals
    • M. Pusey, and R. Naumann Growth kinetics of tetragonal lysozyme crystals J Cryst Growth 76 1986 593 599
    • (1986) J Cryst Growth , vol.76 , pp. 593-599
    • Pusey, M.1    Naumann, R.2
  • 3
    • 0022670426 scopus 로고
    • The growth of large single crystals of lysozyme
    • M. Ataka, and S. Tanaka The growth of large single crystals of lysozyme Biopolymers 25 1986 337 350
    • (1986) Biopolymers , vol.25 , pp. 337-350
    • Ataka, M.1    Tanaka, S.2
  • 4
    • 0024748344 scopus 로고
    • Crystallogenesis of proteins
    • R. Giegé, and V. Mikol Crystallogenesis of proteins Trends Biotechnol 7 1989 277 282
    • (1989) Trends Biotechnol , vol.7 , pp. 277-282
    • Giegé, R.1    Mikol, V.2
  • 5
    • 0036804362 scopus 로고    scopus 로고
    • The genesis of high-throughput structure-based drug discovery using protein crystallography
    • P. Kuhn, K. Wilson, M.G. Patch, and R.C. Stevens The genesis of high-throughput structure-based drug discovery using protein crystallography Curr Opin Chem Biol 6 2002 704 710
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 704-710
    • Kuhn, P.1    Wilson, K.2    Patch, M.G.3    Stevens, R.C.4
  • 6
    • 0037391746 scopus 로고    scopus 로고
    • A procedure for setting up high-throughput nanolitre crystallization experiments. I. Protocol design and validation
    • T.S. Walter, D.J. Brown, M. Pickford, R.J. Owens, D.I. Stuart, and K. Harlos A procedure for setting up high-throughput nanolitre crystallization experiments. I. Protocol design and validation J Appl Crystallogr 36 2003 308 314
    • (2003) J Appl Crystallogr , vol.36 , pp. 308-314
    • Walter, T.S.1    Brown, D.J.2    Pickford, M.3    Owens, R.J.4    Stuart, D.I.5    Harlos, K.6
  • 7
    • 0037394492 scopus 로고    scopus 로고
    • A deliberate approach to screening for initial crystallization conditions of biological macromolecules
    • J.R. Luft, R.J. Collins, N.A. Fehrman, A.M. Lauricella, C.K. Veatch, and G.T. DeTitta A deliberate approach to screening for initial crystallization conditions of biological macromolecules J Struct Biol 142 2003 170 179 A comprehensive description of techniques for high-throughput screening and the robotic visualisation of crystallisation trials.
    • (2003) J Struct Biol , vol.142 , pp. 170-179
    • Luft, J.R.1    Collins, R.J.2    Fehrman, N.A.3    Lauricella, A.M.4    Veatch, C.K.5    Detitta, G.T.6
  • 8
    • 84973021937 scopus 로고
    • Protein crystal growth: An approach based on phase diagram determination
    • M. Ataka Protein crystal growth: an approach based on phase diagram determination Phase Transitions 45 1993 205 219
    • (1993) Phase Transitions , vol.45 , pp. 205-219
    • Ataka, M.1
  • 11
    • 4744353123 scopus 로고    scopus 로고
    • Methods for separating nucleation and growth in protein crystallization
    • in press.
    • Chayen NE: Methods for separating nucleation and growth in protein crystallization. Prog Biophys Mol Biol 2004, in press. A review describing a variety of techniques based on the science of crystallisation for improving crystal quality by manipulation of the crystallisation phase diagram.
    • (2004) Prog Biophys Mol Biol
    • Chayen, N.E.1
  • 12
    • 0348010275 scopus 로고    scopus 로고
    • The 'Octopus' plate for protein crystallization under an electric field
    • C. Charron, C. Didierjean, J.P. Mangeot, and A. Aubry The 'Octopus' plate for protein crystallization under an electric field J Appl Crystallogr 36 2003 1482 1483
    • (2003) J Appl Crystallogr , vol.36 , pp. 1482-1483
    • Charron, C.1    Didierjean, C.2    Mangeot, J.P.3    Aubry, A.4
  • 13
    • 0035502099 scopus 로고    scopus 로고
    • Surface-potential controlled Si-microarray devices for heterogeneous protein crystallization screening
    • A. Sanjoh, T. Tsukihara, and S. Gorti Surface-potential controlled Si-microarray devices for heterogeneous protein crystallization screening J Cryst Growth 232 2001 618 628
    • (2001) J Cryst Growth , vol.232 , pp. 618-628
    • Sanjoh, A.1    Tsukihara, T.2    Gorti, S.3
  • 14
    • 0033886032 scopus 로고    scopus 로고
    • Heterogeneous nucleation of hen egg-white lysozyme - Molecular approach
    • C.N. Nanev, and D. Tsekova Heterogeneous nucleation of hen egg-white lysozyme - molecular approach Cryst Res Technol 35 2000 89 195
    • (2000) Cryst Res Technol , vol.35 , pp. 89-195
    • Nanev, C.N.1    Tsekova, D.2
  • 15
    • 0036075170 scopus 로고    scopus 로고
    • Protein crystallization for genomics: Towards high-throughput optimisation techniques
    • N.E. Chayen, and E. Saridakis Protein crystallization for genomics: towards high-throughput optimisation techniques Acta Crystallogr D Biol Crystallogr 58 2002 921 927
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 921-927
    • Chayen, N.E.1    Saridakis, E.2
  • 17
    • 0037391080 scopus 로고    scopus 로고
    • Seeds to crystals
    • T. Bergfors Seeds to crystals J Struct Biol 142 2003 66 76
    • (2003) J Struct Biol , vol.142 , pp. 66-76
    • Bergfors, T.1
  • 18
    • 0035965131 scopus 로고    scopus 로고
    • Porous silicon: An effective nucleation-inducing material for protein crystallisation
    • N.E. Chayen, E. Saridakis, R. El-Bahar, and Y. Nemirovsky Porous silicon: an effective nucleation-inducing material for protein crystallisation J Mol Biol 312 2001 591 595
    • (2001) J Mol Biol , vol.312 , pp. 591-595
    • Chayen, N.E.1    Saridakis, E.2    El-Bahar, R.3    Nemirovsky, Y.4
  • 19
    • 0037304614 scopus 로고    scopus 로고
    • Systematic improvement of protein crystals by determining the supersolubility curves of phase diagrams
    • E. Saridakis, and N.E. Chayen Systematic improvement of protein crystals by determining the supersolubility curves of phase diagrams Biophys J 84 2003 1218 1222
    • (2003) Biophys J , vol.84 , pp. 1218-1222
    • Saridakis, E.1    Chayen, N.E.2
  • 20
    • 0037291310 scopus 로고    scopus 로고
    • The 1.45 Å three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus
    • J. Nield, P. Rizkallah, J. Barber, and N.E. Chayen The 1.45 Å three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus J Struct Biol 141 2003 149 155
    • (2003) J Struct Biol , vol.141 , pp. 149-155
    • Nield, J.1    Rizkallah, P.2    Barber, J.3    Chayen, N.E.4
  • 21
    • 0027904939 scopus 로고
    • Temperature dependence of protein solubility - Determination and application to crystallization in X-ray capillaries
    • F. Rosenberger, S.B. Howard, J.W. Sowers, and T.A. Nyce Temperature dependence of protein solubility - determination and application to crystallization in X-ray capillaries J Cryst Growth 129 1993 1 12
    • (1993) J Cryst Growth , vol.129 , pp. 1-12
    • Rosenberger, F.1    Howard, S.B.2    Sowers, J.W.3    Nyce, T.A.4
  • 22
  • 23
    • 0343974767 scopus 로고    scopus 로고
    • Thermally induced aggregation of human transferring receptor studied by light-scattering techniques
    • J. Schueler, J. Frank, W. Saenger, and Y. Georgalis Thermally induced aggregation of human transferring receptor studied by light-scattering techniques Biophys J 77 1999 1117 1125
    • (1999) Biophys J , vol.77 , pp. 1117-1125
    • Schueler, J.1    Frank, J.2    Saenger, W.3    Georgalis, Y.4
  • 26
    • 0037392851 scopus 로고    scopus 로고
    • Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination
    • J.D. Ng, J.A. Gavira, and J.M. García-Ruíz Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination J Struct Biol 142 2003 218 231
    • (2003) J Struct Biol , vol.142 , pp. 218-231
    • Ng, J.D.1    Gavira, J.A.2    García-Ruíz, J.M.3
  • 27
    • 0037168508 scopus 로고    scopus 로고
    • A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion
    • C.L. Hansen, E. Skordalakes, J.M. Berger, and S.R. Quak A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion Proc Natl Acad Sci USA 99 2002 16531 16536
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16531-16536
    • Hansen, C.L.1    Skordalakes, E.2    Berger, J.M.3    Quak, S.R.4
  • 28
    • 0031572821 scopus 로고    scopus 로고
    • The role of oil in macromolecular crystallisation
    • N.E. Chayen The role of oil in macromolecular crystallisation Structure 5 1997 1269 1274
    • (1997) Structure , vol.5 , pp. 1269-1274
    • Chayen, N.E.1
  • 31
    • 0036830410 scopus 로고    scopus 로고
    • Tapping DNA for structures produces a trickle
    • R. Service Tapping DNA for structures produces a trickle Science 298 2002 948 950
    • (2002) Science , vol.298 , pp. 948-950
    • Service, R.1
  • 32
    • 4344648879 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins in oils
    • S. Iwata International University Line La Jolla
    • N.E. Chayen Crystallisation of membrane proteins in oils S. Iwata Methods and Results in Crystallization of Membrane Proteins 2003 International University Line La Jolla 131 139
    • (2003) Methods and Results in Crystallization of Membrane Proteins , pp. 131-139
    • Chayen, N.E.1
  • 33
    • 0347692881 scopus 로고    scopus 로고
    • Oils used in microbatch crystallization do not remove a detergent from the drops they cover
    • T.R.M. Barends, and B.W. Dijkstra Oils used in microbatch crystallization do not remove a detergent from the drops they cover Acta Crystallogr D Biol Crystallogr 59 2003 2345 2347
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 2345-2347
    • Barends, T.R.M.1    Dijkstra, B.W.2
  • 34
    • 0037706939 scopus 로고    scopus 로고
    • Compatibility of detergents with the microbatch-under-oil crystallization method
    • P.J. Loll, A. Tretiakova, and E. Soderblom Compatibility of detergents with the microbatch-under-oil crystallization method Acta Crystallogr D Biol Crystallogr 59 2003 1114 1116
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 1114-1116
    • Loll, P.J.1    Tretiakova, A.2    Soderblom, E.3
  • 35
    • 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
  • 36
    • 0037391106 scopus 로고    scopus 로고
    • Macromolecular crystal growth as revealed by atomic force microscopy
    • A. McPherson, Kuznetsov YuG, A. Malkin, and M. Plomp Macromolecular crystal growth as revealed by atomic force microscopy J Struct Biol 142 2003 32 46
    • (2003) J Struct Biol , vol.142 , pp. 32-46
    • McPherson, A.1    Yug Kuznetsov, A.2    Malkin, A.3    Plomp, M.4
  • 37
    • 0036798095 scopus 로고    scopus 로고
    • Effects of a magnetic field and magnetization force on protein crystal growth. Why does a magnet improve the quality of some crystals?
    • M. Ataka, and N.I. Wakayama Effects of a magnetic field and magnetization force on protein crystal growth. Why does a magnet improve the quality of some crystals? Acta Crystallogr D Biol Crystallogr 58 2002 1708 1710
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1708-1710
    • Ataka, M.1    Wakayama, N.I.2
  • 38
    • 0018787717 scopus 로고
    • Protein crystallization using incomplete factorial experiments
    • C.W. Carter Jr., and C.W. Carter Protein crystallization using incomplete factorial experiments J Biol Chem 254 1979 12219 12223
    • (1979) J Biol Chem , vol.254 , pp. 12219-12223
    • Carter Jr., C.W.1    Carter, C.W.2
  • 40
    • 85031083220 scopus 로고    scopus 로고
    • Strategy 2: An alternative to sparse matrix screens
    • T.M. Bergfors International University Line La Jolla
    • M. Ries-Kautt Strategy 2: an alternative to sparse matrix screens T.M. Bergfors Protein Crystallization: Techniques, Strategies, and Tips 1999 International University Line La Jolla 93 110
    • (1999) Protein Crystallization: Techniques, Strategies, and Tips , pp. 93-110
    • Ries-Kautt, M.1
  • 41
    • 0035073346 scopus 로고    scopus 로고
    • Clear strategy screens for macromolecular crystallization
    • A.M. Brzozowski, and J. Walton Clear strategy screens for macromolecular crystallization J Appl Crystallogr 34 2001 97 101
    • (2001) J Appl Crystallogr , vol.34 , pp. 97-101
    • Brzozowski, A.M.1    Walton, J.2
  • 42
    • 0001434101 scopus 로고
    • Crystallizing proteins - A rational approach?
    • A. D'Arcy Crystallizing proteins - a rational approach? Acta Crystallogr D Biol Crystallogr 50 1994 469 471
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 469-471
    • D'Arcy, A.1
  • 44
    • 0037394496 scopus 로고    scopus 로고
    • Light scattering as a diagnostic for protein crystal growth - A practical approach
    • W.W. Wilson Light scattering as a diagnostic for protein crystal growth - a practical approach J Struct Biol 142 2003 56 65 A review of theoretical and experimental considerations concerning the use of a variety of light scattering methods as tools for studying pre- and post-nucleation events, and for predicting favourable crystallisation conditions.
    • (2003) J Struct Biol , vol.142 , pp. 56-65
    • Wilson, W.W.1


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