메뉴 건너뛰기




Volumn 70, Issue 7, 2014, Pages 835-853

Crystallization screening: The influence of history on current practice

Author keywords

crystallization screening

Indexed keywords

PROTEIN;

EID: 84905445266     PISSN: None     EISSN: 2053230X     Source Type: Journal    
DOI: 10.1107/S2053230X1401262X     Document Type: Article
Times cited : (57)

References (138)
  • 1
    • 4344568810 scopus 로고    scopus 로고
    • Protein crystallization and phase diagrams
    • Asherie, N. (2004). Protein crystallization and phase diagrams. Methods, 34, 266-272.
    • (2004) Methods , vol.34 , pp. 266-272
    • Asherie, N.1
  • 3
    • 0027109286 scopus 로고
    • Phase diagrams of a crystalline membrane protein, bovine heart cytochrome c oxidase, in the salting-in region
    • Ataka, M., Shinzawa-Itoh, K. & Yoshikawa, S. (1992). Phase diagrams of a crystalline membrane protein, bovine heart cytochrome c oxidase, in the salting-in region. J. Cryst. Growth, 122, 60-65.
    • (1992) J. Cryst. Growth , vol.122 , pp. 60-65
    • Ataka, M.1    Shinzawa-Itoh, K.2    Yoshikawa, S.3
  • 4
    • 0022670426 scopus 로고
    • The growth of large single crystals of lysozyme
    • Ataka, M. & Tanaka, S. (1986). The growth of large single crystals of lysozyme. Biopolymers, 25, 337-350.
    • (1986) Biopolymers , vol.25 , pp. 337-350
    • Ataka, M.1    Tanaka, S.2
  • 5
    • 0019877808 scopus 로고
    • Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume
    • Atha D.H.,Ingham K.C. (1981). Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume. J. Biol. Chem. 256, 12108-12117.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12108-12117
    • Atha, D.H.1    Ingham, K.C.2
  • 7
    • 0030132944 scopus 로고    scopus 로고
    • A highly efficient 24-condition matrix for the crystallization of nucleic acid fragments
    • Berger, I., Kang, C., Sinha, N.,Wolters, M. & Rich, A. (1996). A highly efficient 24-condition matrix for the crystallization of nucleic acid fragments. Acta Cryst. D52, 465-468.
    • (1996) Acta Cryst. , vol.D52 , pp. 465-468
    • Berger, I.1    Kang, C.2    Sinha, N.3    Wolters, M.4    Rich, A.5
  • 8
    • 0345412741 scopus 로고    scopus 로고
    • Thermodynamics of the hydrophobicity in crystallization of insulin
    • Bergeron, L., Filobelo, L. F., Galkin, O. & Vekilov, P. G. (2003). Thermodynamics of the hydrophobicity in crystallization of insulin. Biophys. J. 85, 3935-3942.
    • (2003) Biophys. J. , vol.85 , pp. 3935-3942
    • Bergeron, L.1    Filobelo, L.F.2    Galkin, O.3    Vekilov, P.G.4
  • 9
    • 0037391080 scopus 로고    scopus 로고
    • Seeds to crystals
    • Bergfors, T. (2003). Seeds to crystals. J. Struct. Biol. 142, 66-76.
    • (2003) J. Struct. Biol. , vol.142 , pp. 66-76
    • Bergfors, T.1
  • 11
    • 0000180941 scopus 로고
    • The purifi cation and crystallization of rennin
    • Berridge, N. J. (1945). The purifi cation and crystallization of rennin. Biochem. J. 39, 179-186.
    • (1945) Biochem. J. , vol.39 , pp. 179-186
    • Berridge, N.J.1
  • 13
    • 0000953383 scopus 로고    scopus 로고
    • Using phase transitions to investigate the effect of salts on protein interactions
    • Broide,M. L., Tominc, T.M. & Saxowsky,M. D. (1996). Using phase transitions to investigate the effect of salts on protein interactions. Phys. Rev. E, 53, 6325-6335.
    • (1996) Phys. Rev. e , vol.53 , pp. 6325-6335
    • Broide, M.L.1    Tominc, T.M.2    Saxowsky, M.D.3
  • 14
    • 0035073346 scopus 로고    scopus 로고
    • Clear strategy screens for macromolecular crystallization
    • Brzozowski, A. M. & Walton, J. (2001). Clear strategy screens for macromolecular crystallization. J. Appl. Cryst. 34, 97-101.
    • (2001) J. Appl. Cryst. , vol.34 , pp. 97-101
    • Brzozowski, A.M.1    Walton, J.2
  • 15
    • 0026116849 scopus 로고
    • Protein solubilities determined by a rapid technique and modification of that technique to a micro-method
    • Cacioppo, E., Munson, S. & Pusey,M. L. (1991). Protein solubilities determined by a rapid technique and modification of that technique to a micro-method. J. Cryst. Growth, 110, 66-71.
    • (1991) J. Cryst. Growth , vol.110 , pp. 66-71
    • Cacioppo, E.1    Munson, S.2    Pusey, M.L.3
  • 16
    • 0028802747 scopus 로고
    • Relative effectiveness of various anions on the solubility of acidic Hypoderma lineatum collagenase at pH 7.2
    • Carbonnaux, C. , Riè s-Kautt, M. & Ducruix, A. (1995). Relative effectiveness of various anions on the solubility of acidic Hypoderma lineatum collagenase at pH 7.2. Protein Sci. 4, 2123-2128.
    • (1995) Protein Sci. , vol.4 , pp. 2123-2128
    • Carbonnaux, C.1    Ries-Kautt, M.2    Ducruix, A.3
  • 17
    • 12644251992 scopus 로고    scopus 로고
    • Response surface methods for optimizing and improving reproducibility of crystal growth
    • Carter, C. W. Jr (1997). Response surface methods for optimizing and improving reproducibility of crystal growth. Methods Enzymol. 276, 74-99.
    • (1997) Methods Enzymol. , vol.276 , pp. 74-99
    • Carter Jr., C.W.1
  • 18
    • 0018787717 scopus 로고
    • Protein crystallization using incomplete factorial experiments
    • Carter, C.W. Jr & Carter, C.W. (1979). Protein crystallization using incomplete factorial experiments. J. Biol. Chem. 254, 12219-12223.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12219-12223
    • Carter Jr., C.W.1    Carter, C.W.2
  • 19
    • 0000383405 scopus 로고
    • Quantitative analysis in the characterization and optimization of protein crystal growth
    • Carter, C. W. Jr & Yin, Y. (1994). Quantitative analysis in the characterization and optimization of protein crystal growth. Acta Cryst. D50, 572-590.
    • (1994) Acta Cryst. , vol.D50 , pp. 572-590
    • Carter Jr., C.W.1    Yin, Y.2
  • 20
    • 79551658540 scopus 로고    scopus 로고
    • Femtosecond X-ray protein nanocrystallography
    • Chapman, H. N. et al. (2011). Femtosecond X-ray protein nanocrystallography. Nature (London), 470, 73-77.
    • (2011) Nature (London) , vol.470 , pp. 73-77
    • Chapman, H.N.1
  • 21
    • 0031936811 scopus 로고    scopus 로고
    • Comparative studies of protein crystallization by vapourdiffusion and microbatch techniques
    • Chayen, N. E. (1998). Comparative studies of protein crystallization by vapourdiffusion and microbatch techniques. Acta Cryst. D54, 8-15.
    • (1998) Acta Cryst. , vol.D54 , pp. 8-15
    • Chayen, N.E.1
  • 22
    • 0024036036 scopus 로고
    • Solubility of glucose isomerase in ammonium sulphate solutions
    • Chayen, N., Akins, J., Campbell-Smith, S. & Blow, D. M. (1988). Solubility of glucose isomerase in ammonium sulphate solutions. J. Cryst. Growth, 90, 112-116.
    • (1988) J. Cryst. Growth , vol.90 , pp. 112-116
    • Chayen, N.1    Akins, J.2    Campbell-Smith, S.3    Blow, D.M.4
  • 23
    • 0027109260 scopus 로고
    • Microbatch crystallization under oil-A new technique allowing many small-volume crystallization trials
    • Chayen, N. E., Shaw Stewart, P. D. & Blow, D. M. (1992). Microbatch crystallization under oil-A new technique allowing many small-volume crystallization trials. J. Cryst. Growth, 122, 176-180.
    • (1992) J. Cryst. Growth , vol.122 , pp. 176-180
    • Chayen, N.E.1    Shaw Stewart, P.D.2    Blow, D.M.3
  • 24
    • 0000192748 scopus 로고
    • An automated system for micro-batch protein crystallization and screening
    • Chayen, N. E., Shaw Stewart, P. D., Maeder, D. L. & Blow, D. M. (1990). An automated system for micro-batch protein crystallization and screening. J. Appl. Cryst. 23, 297-302.
    • (1990) J. Appl. Cryst. , vol.23 , pp. 297-302
    • Chayen, N.E.1    Shaw Stewart, P.D.2    Maeder, D.L.3    Blow, D.M.4
  • 25
    • 0032138631 scopus 로고    scopus 로고
    • Temperature-dependent solubility of selected proteins
    • Christopher, G. K., Phipps, A. G. & Gray, R. J. (1998). Temperature-dependent solubility of selected proteins. J. Cryst. Growth, 191, 820-826.
    • (1998) J. Cryst. Growth , vol.191 , pp. 820-826
    • Christopher, G.K.1    Phipps, A.G.2    Gray, R.J.3
  • 26
    • 0026699340 scopus 로고
    • Purification and crystallization of insecticidal delta-endotoxin CryIIIB2 from Bacillus thuringiensis
    • Cody V.,Luft J.R.,Jensen E.,Pangborn W.,English L. (1992). Purification and crystallization of insecticidal delta-endotoxin CryIIIB2 from Bacillus thuringiensis. Proteins. 14, 324.
    • (1992) Proteins , vol.14 , pp. 324
    • Cody, V.1    Luft, J.R.2    Jensen, E.3    Pangborn, W.4    English, L.5
  • 27
    • 33744494318 scopus 로고    scopus 로고
    • Crystallization optimum solubility screening: Using crystallization results to identify the optimal buffer for protein crystal formation
    • Collins, B., Stevens, R. C. & Page, R. (2005) . Crystallization Optimum Solubility Screening: using crystallization results to identify the optimal buffer for protein crystal formation. Acta Cryst. F61, 1035-1038.
    • (2005) Acta Cryst. , vol.F61 , pp. 1035-1038
    • Collins, B.1    Stevens, R.C.2    Page, R.3
  • 28
    • 16644402929 scopus 로고    scopus 로고
    • A preliminary solubility screen used to improve crystallization trials: Crystallization and preliminary X-ray structure determinat ion of Aeropyrum pernix flap endonuclease-1
    • Collins, B. K., Tomanicek, S. J., Lyamicheva, N., Kaiser, M. W. & Mueser, T. C. (2004). A preliminary solubility screen used to improve crystallization trials: crystallization and preliminary X-ray structure determinat ion of Aeropyrum pernix flap endonuclease-1. Acta Cryst. D60, 1674-1678.
    • (2004) Acta Cryst. , vol.D60 , pp. 1674-1678
    • Collins, B.K.1    Tomanicek, S.J.2    Lyamicheva, N.3    Kaiser, M.W.4    Mueser, T.C.5
  • 29
    • 0024036007 scopus 로고
    • An investigation of protein crystallization parameters using successive automated grid searches (SAGS)
    • Cox, M. J. & Weber, P. C. (1988). An investigation of protein crystallization parameters using successive automated grid searches (SAGS). J. Cryst. Growth, 90, 318-324.
    • (1988) J. Cryst. Growth , vol.90 , pp. 318-324
    • Cox, M.J.1    Weber, P.C.2
  • 30
    • 79952142922 scopus 로고    scopus 로고
    • Protein crystallization and dumb luck
    • Cudney, B. (1999). Protein crystallization and dumb luck. Rigaku J. 16, 1-7.
    • (1999) Rigaku J. , vol.16 , pp. 1-7
    • Cudney, B.1
  • 31
    • 84905479517 scopus 로고    scopus 로고
    • PEG Stability: A Look at pH and Conductivity Changes over Time in Polyethylene Glycols.
    • Cudney, B. (2012). PEG Stability: A Look at pH and Conductivity Changes over Time in Polyethylene Glycols. http://hamptonresearch.com/documents/growth- 101/27.pdf.
    • (2012)
    • Cudney, B.1
  • 32
    • 0003087471 scopus 로고
    • Screening and optimization strategies for macromolecular crystal growth
    • Cudney, R., Patel, S., Weisgraber, K., Newhouse, Y. & McPherson, A. (1994). Screening and optimization strategies for macromolecular crystal growth. Acta Cryst. D50, 414-423.
    • (1994) Acta Cryst. , vol.D50 , pp. 414-423
    • Cudney, R.1    Patel, S.2    Weisgraber, K.3    Newhouse, Y.4    Mc Pherson, A.5
  • 33
    • 0037391084 scopus 로고    scopus 로고
    • The protein as a variable in protein crystallization
    • Dale, G. E., Oefner, C. & D'Arcy, A. (2003). The protein as a variable in protein crystallization. J. Struct. Biol. 142, 88-97.
    • (2003) J. Struct. Biol. , vol.142 , pp. 88-97
    • Dale, G.E.1    Oefner, C.2    D'Arcy, A.3
  • 34
    • 0030565935 scopus 로고    scopus 로고
    • A novel approach to crystallising proteins under oil
    • D'Arcy, A., Elmore, C., Stihle, M. & Johnston, J. (1996). A novel approach to crystallising proteins under oil. J. Cryst. Growth, 168, 175-180.
    • (1996) J. Cryst. Growth , vol.168 , pp. 175-180
    • D'Arcy, A.1    Elmore, C.2    Stihle, M.3    Johnston, J.4
  • 35
    • 4344718651 scopus 로고    scopus 로고
    • Practical aspects of using the microbatch method in screening conditions for protein crystallization
    • D'Arcy, A., MacSweeney, A. & Haber, A. (2004). Practical aspects of using the microbatch method in screening conditions for protein crystallization. Methods, 34, 323-328.
    • (2004) Methods , vol.34 , pp. 323-328
    • D'Arcy, A.1    Mac Sweeney, A.2    Haber, A.3
  • 36
    • 0037321523 scopus 로고    scopus 로고
    • The adVantages of using a modified microbatch method for rapid screening of protein crystallization conditions
    • D'Arcy, A., Mac Sweeney, A., Stihle, M. & Haber , A. (2003). The adVantages of using a modified microbatch method for rapid screening of protein crystallization conditions. Acta Cryst. D59, 396-399.
    • (2003) Acta Cryst. , vol.D59 , pp. 396-399
    • D'Arcy, A.1    Mac Sweeney, A.2    Stihle, M.3    Haber, A.4
  • 37
    • 33947537616 scopus 로고    scopus 로고
    • An automated microseed matrixscreening method for protein crystallization
    • D'Arcy, A., Villard, F. & Marsh, M. (2007). An automated microseed matrixscreening method for protein crystallization. Acta Cryst. D63, 550-554.
    • (2007) Acta Cryst. , vol.D63 , pp. 550-554
    • D'Arcy, A.1    Villard, F.2    Marsh, M.3
  • 38
    • 0026119323 scopus 로고
    • The solubility dependence of canavalin on pH and temperature
    • DeMattei, R. & Feigelson, R. (1991). The solubility dependence of canavalin on pH and temperature. J. Cryst. Growth, 110, 34-40.
    • (1991) J. Cryst. Growth , vol.110 , pp. 34-40
    • De Mattei, R.1    Feigelson, R.2
  • 39
    • 4344584625 scopus 로고    scopus 로고
    • An improved protocol for rapid freezing of protein samples for longterm storage
    • Deng, J., Davies, D. R., Wisedchaisri, G., Wu, M., Hol, W. G. J. & Mehlin, C. (2004). An improved protocol for rapid freezing of protein samples for longterm storage. Acta Cryst. D60, 203-204.
    • (2004) Acta Cryst. , vol.D60 , pp. 203-204
    • Deng, J.1    Davies, D.R.2    Wisedchaisri, G.3    Wu, M.4    Hol, W.G.J.5    Mehlin, C.6
  • 41
    • 0027237520 scopus 로고
    • Crystallization of ribozymes and small RNA motifs by a sparse matrix approach
    • Doudna, J. A., Grosshans, C., Gooding, A. & Kundrot, C. E. (1993). Crystallization of ribozymes and small RNA motifs by a sparse matrix approa ch. Proc. Natl Acad. Sci. USA, 90, 7829-7833.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7829-7833
    • Doudna, J.A.1    Grosshans, C.2    Gooding, A.3    Kundrot, C.E.4
  • 42
    • 61749103757 scopus 로고    scopus 로고
    • Comparative effects of salt, organic, and polymer precipitants on protein phase behavior and implications for vapor diffusion
    • Dumetz, A. C., Chockla, A. M., Kaler, E. W. & Lenhoff, A. M. (2009). Comparative effects of salt, organic, and polymer precipitants on protein phase behavior and implications for vapor diffusion. Cryst. Growth Des. 9, 682-691.
    • (2009) Cryst. Growth Des. , vol.9 , pp. 682-691
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 43
    • 34548427923 scopus 로고    scopus 로고
    • Patterns of protein protein interactions in salt solutions and implications for protein crystallization
    • Dumetz, A. C., Snellinger-O'Brien, A. M., Kaler, E. W. & Lenhoff, A. M. (2007). Patterns of protein protein interactions in salt solutions and implications for protein crystallization. Protein Sci. 16, 1867-1877.
    • (2007) Protein Sci. , vol.16 , pp. 1867-1877
    • Dumetz, A.C.1    Snellinger-O'Brien, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 44
    • 25144438551 scopus 로고    scopus 로고
    • A modified vapor-diffusion crystallization protocol that uses a common dehydrating agent
    • Dunlop, K. V. & Hazes, B. (2005). A modified vapor-diffusion crystallization protocol that uses a common dehydrating agent. Acta Cryst. D61, 1041-1048.
    • (2005) Acta Cryst. , vol.D61 , pp. 1041-1048
    • Dunlop, K.V.1    Hazes, B.2
  • 45
    • 80955136787 scopus 로고    scopus 로고
    • A thermal stability assay can help to estimate the crystallization likelihood of biological samples
    • Dupeux , F., Röwer, M., Seroul, G., Blot, D. Márquez, J. A. (2011). A thermal stability assay can help to estimate the crystallization likelihood of biological samples. Acta Cryst. D67, 915-919.
    • (2011) Acta Cryst. , vol.D67 , pp. 915-919
    • Dupeux, F.1    Rower, M.2    Seroul, G.3    Blot, D.4    Marquez, J.A.5
  • 46
    • 16544384999 scopus 로고    scopus 로고
    • Assessing crystallization droplets using birefringence
    • Echalier, A., Glazer, R. L., Fülöp, V. & Geday, M. A. (2004). Assessing crystallization droplets using birefringence. Acta Cryst. D60, 696-702.
    • (2004) Acta Cryst. , vol.D60 , pp. 696-702
    • Echalier, A.1    Glazer, R.L.2    Fulop, V.3    Geday, M.A.4
  • 47
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson, U. B., Hallberg, B. M., D eTitta, G. T., Dekker, N. & Nordlund, P. (2006). Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357, 289-298.
    • (2006) Anal. Biochem. , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    De Titta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 48
    • 0000488635 scopus 로고
    • Orthorhombic lysozyme solubility
    • Ewing F.,Forsythe E.,Pusey M. (1994). Orthorhombic lysozyme solubility. Acta Cryst. D50, 424-428.
    • (1994) Acta Cryst. , vol.D50 , pp. 424-428
    • Ewing, F.1    Forsythe, E.2    Pusey, M.3
  • 49
    • 0027372495 scopus 로고
    • Crystallization of Old Yellow Enzyme illustrates an effective strategy for increasing protein crystal size
    • Fox, K. M. & Karplus, P. A. (1993). Crystallization of Old Yellow Enzyme illustrates an effective strategy for increasing protein crystal size. J. Mol. Biol. 234, 502-507.
    • (1993) J. Mol. Biol. , vol.234 , pp. 502-507
    • Fox, K.M.1    Karplus, P.A.2
  • 50
    • 0344665696 scopus 로고    scopus 로고
    • Counterdiffusion methods for macromolecular crystallization
    • García-Ruiz, J. M. (2003). Counterdiffusion methods for macromolecular crystallization. Methods Enzymol. 368, 130-154.
    • (2003) Methods Enzymol. , vol.368 , pp. 130-154
    • Garcia-Ruiz, J.M.1
  • 51
    • 0000449985 scopus 로고    scopus 로고
    • Glycerol concentrations required for cryoprotection of 50 typical protein crystallization solutions
    • Garman, E. F. & Mitchell, E. P. (1996). Glycerol concentrations required for cryoprotection of 50 typical protein crystallization solutions. J. Appl. Cryst. 29, 584-587.
    • (1996) J. Appl. Cryst. , vol.29 , pp. 584-587
    • Garman, E.F.1    Mitchell, E.P.2
  • 52
    • 0343035631 scopus 로고    scopus 로고
    • Solubility diagram of the rhodobacter sphaeroides reaction center as a function of PEG concentration
    • Gaucher, J.-F., Riè s-Kautt, M., Reiss-Hu sson, F. & Ducruix, A. (1997). Solubility diagram of the Rhodobacter sphaeroides reaction center as a function of PEG concentration. FEBS Lett. 401, 113-116.
    • (1997) FEBS Lett. , vol.401 , pp. 113-116
    • Gaucher, J.-F.1    Ries-Kautt, M.2    Reiss-Husson, F.3    Ducruix, A.4
  • 53
    • 84889636867 scopus 로고    scopus 로고
    • A historical perspective on protein crystallization from 1840 to the present day
    • Giegé, R. (2013). A historical perspective on protein crystallization from 1840 to the present day. FEBS J. 280, 6456-6497.
    • (2013) FEBS J. , vol.280 , pp. 6456-6497
    • Giege, R.1
  • 54
    • 0024037620 scopus 로고
    • A biological macromolecule crystallization database: A basis for a crystallization strategy
    • Gilliland, G. L. (1988). A biological macromolecule crystallization database: A basis for a crystallization strategy. J. Cryst. Growth, 90, 51-59.
    • (1988) J. Cryst. Growth , vol.90 , pp. 51-59
    • Gilliland, G.L.1
  • 55
    • 0000898340 scopus 로고
    • Biological macromolecule crystallization database, Version 3.0: New features, data and the NASA archive for protein crystal growth data
    • Gilliland, G. L., Tung, M., Blakeslee, D. M. & Ladner, J. E. (1994). Biological Macromolecule Crystallization Database, Version 3.0: new features, data and the NASA archive for protein crystal growth dat a. Acta Cryst. D50, 408-413.
    • (1994) Acta Cryst. , vol.D50 , pp. 408-413
    • Gilliland, G.L.1    Tung, M.2    Blakeslee, D.M.3    Ladner, J.E.4
  • 57
    • 70449768051 scopus 로고    scopus 로고
    • The MORPHEUS protein crystallization screen
    • Gorrec, F. (200 9). The MORPHEUS protein crystallization screen. J. Appl. Cryst. 42, 1035-1042.
    • (2009) J. Appl. Cryst. , vol.42 , pp. 1035-1042
    • Gorrec, F.1
  • 58
    • 0000116343 scopus 로고
    • Studies in the physical chemistry of the proteins: VIII. The solubility of hemoglobin in concentrated salt solutions. A study of the salting out of proteins
    • Green, A. A. (1931). Studies in the physical chemistry of the proteins: VIII. The solubility of hemoglobin in concentrated salt soluti ons. A study of the salting out of proteins. J. Biol. Chem. 93, 495-516.
    • (1931) J. Biol. Chem. , vol.93 , pp. 495-516
    • Green, A.A.1
  • 59
    • 0028846780 scopus 로고
    • Crystallization of intact monoclonal antibodies
    • Harris, L. J., Skaletsky, E. & McPherson, A. (1995). Crystallization of intact monoclonal antibodies. Proteins, 23, 285-289.
    • (1995) Proteins , vol.23 , pp. 285-289
    • Harris, L.J.1    Skaletsky, E.2    Mc Pherson, A.3
  • 60
    • 0033936978 scopus 로고    scopus 로고
    • Statistical methods for the objective design of screening procedures for macromolecular crystallization
    • Hennessy, D., Buchanan, B., Subramanian, D., Wilkosz, P. A. & Rosenberg, J. M. (2000). Statistical methods for the objective design of screening procedures for macromolecular crystallization. Acta C ryst. D56, 817-827.
    • (2000) Acta Cryst. , vol.D56 , pp. 817-827
    • Hennessy, D.1    Buchanan, B.2    Subramanian, D.3    Wilkosz, P.A.4    Rosenberg, J.M.5
  • 61
    • 84905479511 scopus 로고
    • Die Chemismus in der Thierischen Organization Leipzig: Brockhaus
    • Hünefeld, F. L. (1840). Die Chemismus in der Thierischen Organization, p. 160. Leipzig: Brockhaus.
    • (1840) , pp. 160
    • Hunefeld, F.L.1
  • 62
    • 7444264009 scopus 로고    scopus 로고
    • Microseed matrix screening to improve crystals of yeast cytosine deaminase
    • Ireton, G. C. & Stoddard, B. L. (2004). Microseed matrix screening to improve crystals of yeast cytosine deaminase. Acta Cryst. D60, 601-605.
    • (2004) Acta Cryst. , vol.D60 , pp. 601-605
    • Ireton, G.C.1    Stoddard, B.L.2
  • 63
    • 33745644237 scopus 로고    scopus 로고
    • Assessment of a preliminary solubility screen to improve crystallizati on trials: Uncoupling crystal condition searches
    • Izaac, A., Schall, C. A. & Mueser, T. C. (2006). Assessment of a preliminary solubility screen to improve crystallizati on trials: uncoupling crystal condition searches. Acta Cryst. D62, 833-842.
    • (2006) Acta Cryst. , vol.D62 , pp. 833-842
    • Izaac, A.1    Schall, C.A.2    Mueser, T.C.3
  • 64
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J. & Kim, S.-H. (1991). Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Cryst. 24, 409-411.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 65
    • 16644371341 scopus 로고    scopus 로고
    • Optimum solubility (OS) screening: An efficient method to optimize buffer conditions for homogeneity and crystallization of pr oteins
    • Jancarik, J., Pufan, R., Hong, C., Kim, S.-H. & Kim, R. (2004). Optimum solubility (OS) screening: an efficient method to optimize buffer conditions for homogeneity and crystallization of pr oteins. Acta Cryst. D60, 1670-1673.
    • (2004) Acta Cryst. , vol.D60 , pp. 1670-1673
    • Jancarik, J.1    Pufan, R.2    Hong, C.3    Kim, S.-H.4    Kim, R.5
  • 66
    • 0014403212 scopus 로고
    • Alcohol oxidase a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyethylene glycol
    • Janssen, F. W. & Ruelius, H. W. (1968). Alcohol oxidase, a flavoprotein from several Basidiomycetes species. Crystallization by fractional precipitation with polyeth ylene glycol. Biochim. Biophys. Acta, 151, 330-342.
    • (1968) Biochim. Biophys. Acta , vol.151 , pp. 330-342
    • Janssen, F.W.1    Ruelius, H.W.2
  • 68
    • 0000122663 scopus 로고
    • Search designs for protein crystallization based on orthogonal arrays
    • Kingston, R. L., Baker, H. M. & Baker, E. N. (1994). Search designs for protein crystallization based on orthogonal arrays. Acta Cryst. D50, 429-440.
    • (1994) Acta Cryst. , vol.D50 , pp. 429-440
    • Kingston, R.L.1    Baker, H.M.2    Baker, E.N.3
  • 69
    • 4444275437 scopus 로고    scopus 로고
    • Zur lehre von der wirkung der salze (about the science of the effect of salts): Franz hofmeister's historical papers
    • Kunz W.,Henle J.,Ninham B.W. (2004). Zur lehre von der wirkung der salze (about the science of the effect of salts): Franz hofmeister's historical papers. Curr. Opin. Colloid Interface Sci. 9, 19-37.
    • (2004) Curr. Opin. Colloid Interface Sci. , vol.9 , pp. 19-37
    • Kunz, W.1    Henle, J.2    Ninham, B.W.3
  • 70
    • 0015523222 scopus 로고
    • Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast
    • Lagerkvist, U., Rymo, L., Lindqvist, O. & Andersson, E. (1972). Some properties of crystals of lysine transfer ribonucleic acid ligase from yeast. J. Biol. Chem. 247, 3897-3899.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3897-3899
    • Lagerkvist, U.1    Rymo, L.2    Lindqvist, O.3    Andersson, E.4
  • 71
    • 61549093735 scopus 로고    scopus 로고
    • Progress in the development of an alternative approach to macromolecular crystallization
    • Larson, S. B., Day, J. S., Nguyen, C., Cudney, R. & McPherson, A. (2008). Progress in the development of an alternative approach to macromolecular crystallization. Cryst. Growth Des. 8, 3038-3052.
    • (2008) Cryst. Growth Des. , vol.8 , pp. 3038-3052
    • Larson, S.B.1    Day, J.S.2    Nguyen, C.3    Cudney, R.4    Mc Pherson, A.5
  • 72
    • 3442885098 scopus 로고    scopus 로고
    • A modified microdialysis button for use in protein crystallization
    • Lee, S. S. J. & Cudney, R. (2004). A modified microdialysis button for use in protein crystallization. J. Appl. Cryst. 37, 504-505.
    • (2004) J. Appl. Cryst. , vol.37 , pp. 504-505
    • Lee, S.S.J.1    Cudney, R.2
  • 73
    • 0030515942 scopus 로고    scopus 로고
    • The rate of water equilibration in vapor-diffusion crystallizations: Dependence on the distance from the droplet to the reservoir
    • Luft, J. R., Albright, D. T., Baird, J. K. & DeTitta, G. T. (1996). The rate of water equilibration in vapor-diffusion crystallizations: dependence on the distance from the droplet to the reservoir. Acta Cryst. D52, 1098-1106.
    • (1996) Acta Cryst. , vol.D52 , pp. 1098-1106
    • Luft, J.R.1    Albright, D.T.2    Baird, J.K.3    De Titta, G.T.4
  • 74
    • 0028483512 scopus 로고
    • A macromolecular crystallization procedure employing diffusion cells of varying depths as reservoirs to tailor the time course of equilibration in hanging-and sitting-drop vapor-diffusion and microdialysis experiments
    • Luft, J. R., Arakali, S. V., Kirisits, M. J., Kalenik, J. ., Wawrzak, I., Cody, V., Pangborn, W. A. & DeTitta, G. T. (1994). A macromolecular crystallization procedure employing diffusion cells of varying depths as reservoirs to tailor the time course of equilibration in hanging-and sitting-drop vapor-diffusion and microdialysis experiments. J. Appl. Cryst. 27, 443-452.
    • (1994) J. Appl. Cryst. , vol.27 , pp. 443-452
    • Luft, J.R.1    Arakali, S.V.2    Kirisits, M.J.3    Kalenik, J.4    Wawrzak, I.5    Cody, V.6    Pangborn, W.A.7    De Titta, G.T.8
  • 75
    • 0031052837 scopus 로고    scopus 로고
    • Kinetic aspects of macromolecular crystallization
    • Luft, J. R. & DeTitta, G. (1997). Kinetic aspects of macromolecular crystallization. Methods Enzymol., 276, 110-131.
    • (1997) Methods Enzymol. , vol.276 , pp. 110-131
    • Luft, J.R.1    De Titta, G.2
  • 76
    • 77957365948 scopus 로고    scopus 로고
    • 2nd ed., edited by T. M. Bergfors LaJolla: International University Line.
    • Luft, J. R. & DeTitta, G. T. (2009). Protein Crystallization, 2nd ed., edited by T. M. Bergfors, pp. 11-40. LaJolla: International University Line.
    • (2009) Protein Crystallization , pp. 11-40
    • Luft, J.R.1    De Titta, G.T.2
  • 77
    • 0033513760 scopus 로고    scopus 로고
    • Microbatch macromolecular crystallization on a thermal gradient
    • Luft, J. R., Rak, D. M. & DeTitta, G. T. (19 99). Microbatch macromolecular crystallization on a thermal gradient. J. Cryst. Growth, 196, 447-449.
    • (1999) J. Cryst. Growth , vol.196 , pp. 447-449
    • Luft, J.R.1    Rak, D.M.2    De Titta, G.T.3
  • 78
    • 79955442040 scopus 로고    scopus 로고
    • Lessons from high-throughput protein crystallization screening: 1 0 years of practical experience
    • Luft, J. R., Snell, E. H. & DeTitta, G. T. (2011). Lessons from high-throughput protein crystallization screening: 1 0 years of practical experience. Expert Opin. Drug Discov. 6, 465-480.
    • (2011) Expert Opin. Drug Discov. , vol.6 , pp. 465-480
    • Luft, J.R.1    Snell, E.H.2    De Titta, G.T.3
  • 80
    • 79952180427 scopus 로고    scopus 로고
    • What's in a drop? Correlating observations and outcomes to guide macromolecular crystallization experiments
    • Luft, J. R., Wolfley, J. R. & Snell, E. H. (2011). What's in a drop? Correlating observations and outcomes to guide macromolecular crystallization experiments. Cryst. Growth Des. 11, 651-663.
    • (2011) Cryst. Growth Des. , vol.11 , pp. 651-663
    • Luft, J.R.1    Wolfley, J.R.2    Snell, E.H.3
  • 81
    • 0041333138 scopus 로고    scopus 로고
    • Enhancing protein crystallization through precipitant synergy
    • Majeed, S., Ofek, G., Belachew, A., Huang, C.-C., Zhou, T. & Kwong, P. D. (2003). Enhancing protein crystallization through precipitant synergy. Structure, 11, 1061-1070.
    • (2003) Structure , vol.11 , pp. 1061-1070
    • Majeed, S.1    Ofek, G.2    Belachew, A.3    Huang, C.-C.4    Zhou, T.5    Kwong, P.D.6
  • 83
    • 0017202693 scopus 로고
    • Crystallization of proteins from polyethylene glycol
    • McPherson, A. Jr (1976 a ). Crystallization of proteins from polyethylene glycol. J. Biol. Chem. 251, 6300-6303.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6300-6303
    • Mc Pherson Jr., A.1
  • 84
    • 0017219062 scopus 로고
    • The growth and preliminary investigation of protein and nu cleic acid crystals for X-ray diffraction analysis
    • McPherson, A. Jr (1976 b). The growth and preliminary investigation of protein and nu cleic acid crystals for X-ray diffraction analysis. Methods Biochem. Anal. 23, 249-345.
    • (1976) Methods Biochem. Anal. , vol.23 , pp. 249-345
    • Mc Pherson Jr., A.1
  • 86
    • 0027109318 scopus 로고
    • Two approaches to the rapid screening of crystallization conditions
    • McPherson, A. (1992). Two approaches to the rapid screening of crystallization conditions. J. Cryst. Growth, 122, 161-167.
    • (1992) J. Cryst. Growth , vol.122 , pp. 161-167
    • Mc Pherson, A.1
  • 87
    • 0001259632 scopus 로고
    • Increasing the size of microcrystals by fine sampling of pH limits
    • McPherson, A. (1995). Increasing the size of microcrystals by fine sampling of pH limits. J. Appl. Cryst. 28, 362-365.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 362-365
    • Mc Pherson, A.1
  • 88
    • 33751000441 scopus 로고    scopus 로고
    • Searching for silver bullets: An alternative strategy for crystallizing macromolecules
    • McPherson, A. & Cudney, B. (2006). Searching for silver bullets: an alternative strategy for crystallizing macromolecules. J. Struct. Biol. 156, 387-406.
    • (2006) J. Struct. Biol. , vol.156 , pp. 387-406
    • Mc Pherson, A.1    Cudney, B.2
  • 89
    • 84902828502 scopus 로고    scopus 로고
    • Introduction to protein crystallization
    • McPherson, A. & Gavira, J. A. (2014). Introduction to protein crystallization. Acta Cryst. F70, 2-20.
    • (2014) Acta Cryst. , vol.F70 , pp. 2-20
    • Mc Pherson, A.1    Gavira, J.A.2
  • 91
    • 0024737404 scopus 로고
    • Phase diagram of a crystalline protein: Determination of the solubility of concanavalin A by a microquantitation assay
    • Mikol V.,Giege R. (1989). Phase diagram of a crystalline protein: Determination of the solubility of concanavalin A by a microquantitation assay. J. Cryst. Growth. 97, 324-332.
    • (1989) J. Cryst. Growth , vol.97 , pp. 324-332
    • Mikol, V.1    Giege, R.2
  • 92
    • 7444225775 scopus 로고    scopus 로고
    • Novel buffer systems for macromolecular crystallization
    • Newman, J. (2004). Novel buffer systems for macromolecular crystallization. Acta Cryst. D60, 610-612.
    • (2004) Acta Cryst. , vol.D60 , pp. 610-612
    • Newman, J.1
  • 93
    • 23844452138 scopus 로고    scopus 로고
    • Expanding screening space through the use of alternative reservoirs in vapor-diffusion experiments
    • Newman, J. (2005). Expanding screening space through the use of alternative reservoirs in vapor-diffusion experiments. Acta Cryst. D61, 490-493.
    • (2005) Acta Cryst. , vol.D61 , pp. 490-493
    • Newman, J.1
  • 96
    • 32944460868 scopus 로고    scopus 로고
    • Towards rationalization of crystallization screen ing for small-to medium-sized academic laboratories: The PACT/JCSG+ strategy
    • Newman, J., Egan, D., Walter, T. S., Meged, R., Berry, I., Ben Jelloul, M., Sussman, J. L., Stuart, D. I. & Perrakis, A. (2005). Towards rationalization of crystallization screen ing for small-to medium-sized academic laboratories: the PACT/JCSG+ strategy. Acta Cryst. D61, 1426-1431.
    • (2005) Acta Cryst. , vol.D61 , pp. 1426-1431
    • Newman, J.1    Egan, D.2    Walter, T.S.3    Meged, R.4    Berry, I.5    Ben Jelloul, M.6    Sussman, J.L.7    Stuart, D.I.8    Perrakis, A.9
  • 97
    • 71949100268 scopus 로고    scopus 로고
    • Pract ical aspects of the SAMPL challenge: Providing an extensive experimental data set for the modeling community
    • Newman, J., Fazio, V. J., Caradoc-Davies, T. T., Branson, K. & Peat, T. S. (2009). Pract ical aspects of the SAMPL challenge: providing an extensive experimental data set for the modeling community. J. Biomol. Screen. 14, 1245-1250.
    • (2009) J. Biomol. Screen. , vol.14 , pp. 1245-1250
    • Newman, J.1    Fazio, V.J.2    Caradoc-Davies, T.T.3    Branson, K.4    Peat, T.S.5
  • 98
    • 77953156113 scopus 로고    scopus 로고
    • The C6 web tool: A resource for the rational selection of crystallization conditions
    • Newman, J., Fazio, V. J., Lawson, B. & Peat, T. S. (2010). The C6 web tool: a resource for the rational selection of crystallization conditions. Cryst. Growth Des. 10, 2785-2792.
    • (2010) Cryst. Growth Des. , vol.10 , pp. 2785-2792
    • Newman, J.1    Fazio, V.J.2    Lawson, B.3    Peat, T.S.4
  • 99
    • 78651076181 scopus 로고    scopus 로고
    • Crystallization of an apo form of human arginase: Using all the tools in the toolbox simultaneously
    • Newman, J., Pearce, L., Lesburg, C. A., Strickland, C. & Peat, T. S. (2011). Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously. Acta Cryst. F67, 90-93.
    • (2011) Acta Cryst. , vol.F67 , pp. 90-93
    • Newman, J.1    Pearce, L.2    Lesburg, C.A.3    Strickland, C.4    Peat, T.S.5
  • 100
    • 55949129694 scopus 로고    scopus 로고
    • Phoenito experiments: Combining the strengths of commercial crystallization automation
    • Newman, J., Pham, T.M. & Peat, T. S. (2008). Phoenito experiments: combining the strengths of commercial crystallization automation. Acta Cryst. F64, 991-996.
    • (2008) Acta Cryst. , vol.F64 , pp. 991-996
    • Newman, J.1    Pham, T.M.2    Peat, T.S.3
  • 101
    • 34250809692 scopus 로고    scopus 로고
    • Initial evaluations of the reproducibility of vapor-diffusion crystallization
    • Newman, J., Xu, J. & Willis, M. C. (2007). Initial evaluations of the reproducibility of vapor-diffusion crystallization. Acta Cryst. D63, 826-832.
    • (2007) Acta Cryst. , vol.D63 , pp. 826-832
    • Newman, J.1    Xu, J.2    Willis, M.C.3
  • 102
    • 39549108859 scopus 로고    scopus 로고
    • Rationalizing-helical membrane protein crystallization
    • Newstead, S., Ferrandon, S. & Iwata, S. (2008). Rationalizing-helical membrane protein crystallization. Protein Sci. 17, 466-472.
    • (2008) Protein Sci. , vol.17 , pp. 466-472
    • Newstead, S.1    Ferrandon, S.2    Iwata, S.3
  • 103
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F. H., Berglund, H. & Vedadi, M. (2007). The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nature Protoc. 2, 2212-2221.
    • (2007) Nature Protoc. , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 104
    • 77955452253 scopus 로고    scopus 로고
    • Promoting crystallization of antibody-antigen complexes via microseed matrix screening
    • Obmolova, G., Malia, T. J., Teplyakov, A., Sweet, R. & Gilliland, G. L. (2010). Promoting crystallization of antibody-antigen complexes via microseed matrix screening. Acta Cryst. D66, 927-933.
    • (2010) Acta Cryst. , vol.D66 , pp. 927-933
    • Obmolova, G.1    Malia, T.J.2    Teplyakov, A.3    Sweet, R.4    Gilliland, G.L.5
  • 105
    • 0013434758 scopus 로고
    • The protein constituents of egg white
    • Osborne, T. B. & Campbell, G. F. (1900). The protein constituents of egg white. J. Am. Chem. Soc. 22, 422-450.
    • (1900) J. Am. Chem. Soc. , vol.22 , pp. 422-450
    • Osborne, T.B.1    Campbell, G.F.2
  • 106
    • 0038384417 scopus 로고    scopus 로고
    • Shotgun crystallization strategy for structural genomics: An optimized two-tiered crystallization screen against the Thermotoga mariti ma proteome
    • Page, R., Grzechnik, S. K., Cana ves, J. M., Spraggon, G., Kreusch, A., Kuhn, P., Stevens, R. C. & Lesley, S. A. (2003). Shotgun crystallization strategy for structural genomics: an optimized two-tiered crystallization screen against the Thermotoga mariti ma proteome. Acta Cryst. D59, 1028-1037.
    • (2003) Acta Cryst. , vol.D59 , pp. 1028-1037
    • Page, R.1    Grzechnik, S.K.2    Canaves, J.M.3    Spraggon, G.4    Kreusch, A.5    Kuhn, P.6    Stevens, R.C.7    Lesley, S.A.8
  • 107
    • 4344570209 scopus 로고    scopus 로고
    • Crystallization data mining in structural genomics: Using positive and negative results to optimize protein crystallization screens
    • Page, R. & Stevens, R. C. (2004). Crystallization data mining in structural genomics: using positive and negative results to optimize protein crystallization screens. Methods, 34, 373-389.
    • (2004) Methods , vol.34 , pp. 373-389
    • Page, R.1    Stevens, R.C.2
  • 108
    • 84865409390 scopus 로고    scopus 로고
    • Current trends in-helical membrane protein crystallization: An update
    • Parker, J. L. & Newstead, S. (2012). Current trends in-helical membrane protein crystallization: an update. Protein Sci. 21, 1358-1365.
    • (2012) Protein Sci. , vol.21 , pp. 1358-1365
    • Parker, J.L.1    Newstead, S.2
  • 109
    • 33644848209 scopus 로고    scopus 로고
    • Tapping the Protein Data Bank for crystallization information
    • Peat, T. S., Chris topher, J. A. & Newman, J. (2005). Tapping the Protein Data Bank for crystallization information. Acta Cryst. D61, 1662-1669.
    • (2005) Acta Cryst. , vol.D61 , pp. 1662-1669
    • Peat, T.S.1    Christopher, J.A.2    Newman, J.3
  • 111
    • 59349103076 scopus 로고    scopus 로고
    • Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data
    • Price, W. N. II et al. (2009). Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data. Nature Biotechnol. 27, 51-57.
    • (2009) Nature Biotechnol. , vol.27 , pp. 51-57
    • Price, I.I.W.N.1
  • 112
    • 34247466556 scopus 로고    scopus 로고
    • Protein crystallization using room temperature ionic liquids
    • Pusey, M. L., Paley, M. S., Turner, M. B. & Rogers, R. D. (2007). Protein crystallization using room temperature ionic liquids. Cryst. Growth Des. 7, 787-793.
    • (2007) Cryst. Growth Des. , vol.7 , pp. 787-793
    • Pusey, M.L.1    Paley, M.S.2    Turner, M.B.3    Rogers, R.D.4
  • 113
    • 0036894186 scopus 로고    scopus 로고
    • Crystallization of protein-protein complexes
    • Radaev S.,Sun P.D. (2002). Crystallization of protein-protein complexes. J. Appl. Cryst. 35, 674-676.
    • (2002) J. Appl. Cryst. , vol.35 , pp. 674-676
    • Radaev, S.1    Sun, P.D.2
  • 114
    • 0027904939 scopus 로고
    • Temperature dependence of protein solubility-determination and application to crystallization in X-ray capillaries
    • Rosenberger, F., Howard, S. B., Sowers, J. W. & Nyce, T. A. (1993). Temperature dependence of protein solubility-determination and application to crystallization in X-ray capillaries. J. Cryst. Growth, 129, 1-1 2.
    • (1993) J. Cryst. Growth , vol.129 , pp. 1-12
    • Rosenberger, F.1    Howard, S.B.2    Sowers, J.W.3    Nyce, T.A.4
  • 115
    • 0015386003 scopus 로고
    • A free interface diffusion technique for the crystallization of proteins for X-ray crystallography
    • Salemme, F. R. (1972). A free interface diffusion technique for the crystallization of proteins for X-ray crystallography. Arch. Biochem. Biophys. 151, 533-539.
    • (1972) Arch. Biochem. Biophys. , vol.151 , pp. 533-539
    • Salemme, F.R.1
  • 116
    • 0026926895 scopus 로고
    • Cluster analysis of the biological macromolecule crystallization database
    • Samudzi, C. T., Fivash, M. J. & Rosenberg, J. M. (1992). Cluster analysis of the Biological Macromolecule Crystallization Database. J. Cryst. Growth, 123, 47-58.
    • (1992) J. Cryst. Growth , vol.123 , pp. 47-58
    • Samudzi, C.T.1    Fivash, M.J.2    Rosenberg, J.M.3
  • 117
    • 0028103071 scopus 로고
    • Phase diagram and dilution experiments in the crystallization of carboxypeptidase G2
    • Saridakis, E. E. G., Shaw Stewart, P. D., Lloyd, L. F. & Blow, D. M. (1994). Phase diagram and dilution experiments in the crystallization of carboxypeptidase G2. Acta Cryst. D50, 293-297.
    • (1994) Acta Cryst. , vol.D50 , pp. 293-297
    • Saridakis, E.E.G.1    Shaw Stewart, P.D.2    Lloyd, L.F.3    Blow, D.M.4
  • 119
    • 0029115376 scopus 로고
    • Rapid crystallization of chemically synthesized hammerhead RNAs using a double screening procedure
    • Scott,W. G., Finch, J. T., Grenfell, R., Fogg, J., Smith, T., Gait, M. J. & Klug, A. (1995). Rapid crystallization of chemically synthesized hammerhead RNAs using a double screening pr ocedure. J. Mol. Biol. 250, 327-332.
    • (1995) J. Mol. Biol. , vol.250 , pp. 327-332
    • Scott, W.G.1    Finch, J.T.2    Grenfell, R.3    Fogg, J.4    Smith, T.5    Gait, M.J.6    Klug, A.7
  • 120
    • 0035501932 scopus 로고    scopus 로고
    • Efficiency analysis of sampling protocols used in protein crystallization screening
    • Segelke, B. W. (2001). Efficiency analysis of sampling protocols used in protein crystallization screening. J. Cryst. Growth, 232, 553-562.
    • (2001) J. Cryst. Growth , vol.232 , pp. 553-562
    • Segelke, B.W.1
  • 124
    • 56549105156 scopus 로고    scopus 로고
    • The application and use of chemical space mapping to interpret crystallization screening results
    • Snell, E. H., Nagel, R. M., Wojtaszcyk, A., O'Neill, H., Wolfley, J. L. & Luft, J. R. (2008). The application and use of chemical space mapping to interpret crystallization screening results. Acta Cryst. D64, 1240-1249 .
    • (2008) Acta Cryst. , vol.D64 , pp. 1240-1249
    • Snell, E.H.1    Nagel, R.M.2    Wojtaszcyk, A.3    O'Neill, H.4    Wolfley, J.L.5    Luft, J.R.6
  • 126
    • 0029108966 scopus 로고
    • Use of glycerol, polyols and other protein structure stabilizing agents in protein crystallization
    • Sousa, R. (1995). Use of glycerol, polyols and other protein structure stabilizing agents in protein crystallization. Acta Cryst. D51, 271-277.
    • (1995) Acta Cryst. , vol.D51 , pp. 271-277
    • Sousa, R.1
  • 127
    • 0027109248 scopus 로고
    • Strategies in the crystallization of glycoproteins and protein complexes
    • Stura, E. A., Nemerow, G. R. & Wilson, I. A. (1992). Strategies in the crystallization of glycoproteins and protein complexes. J. Cryst. Growth, 122, 273-285.
    • (1992) J. Cryst. Growth , vol.122 , pp. 273-285
    • Stura, E.A.1    Nemerow, G.R.2    Wilson, I.A.3
  • 129
    • 0013793601 scopus 로고
    • Evidence for virusspecific noncapsid proteins in poliovirus-infected HeLa cells
    • Summers, D. F., Maizel, J. V. Jr & Darnell, J. E. Jr (1965). Evidence for virusspecific noncapsid proteins in poliovirus-infected HeLa cells. Proc. Natl Acad. Sci. USA, 54, 505-513.
    • (1965) Proc. Natl Acad. Sci. USA , vol.54 , pp. 505-513
    • Summers, D.F.1    Maizel Jr., J.V.2    Darnell Jr., J.E.3
  • 130
    • 0001470914 scopus 로고
    • The isolation and crystallization of the enzyme urease: Preliminary paper
    • Sumner, J. B. (1926). The isolation and crystallization of the enzyme urease: preliminary paper. J. Biol. Chem. 69, 435-441.
    • (1926) J. Biol. Chem. , vol.69 , pp. 435-441
    • Sumner, J.B.1
  • 133
    • 16644403384 scopus 로고    scopus 로고
    • Statistical experimental design of protein crystallization screening revisited
    • Tran, T. T., Sorel, I. & Lewit-Bentley, A. (2004). Statistical experimental design of protein crystallization screening revisited. Acta Cryst. D60, 1562-1568.
    • (2004) Acta Cryst. , vol.D60 , pp. 1562-1568
    • Tran, T.T.1    Sorel, I.2    Lewit-Bentley, A.3
  • 134
    • 58549110253 scopus 로고    scopus 로고
    • The Biomolecular Crystallization Database Version 4: Expanded content and new features
    • Tung M.,Gallagher D.T. (2009). The Biomolecular Crystallization Database Version 4: expanded content and new features. Acta Cryst. D65, 18-23.
    • (2009) Acta Cryst. , vol.D65 , pp. 18-23
    • Tung, M.1    Gallagher, D.T.2
  • 135
    • 8844226743 scopus 로고    scopus 로고
    • Temperature and pH effect on the polymorphism of aprotinin (BPTI) in sodium bromide solutions
    • Veesler, S., Ferte, N., Costes, M. S., Czjzek, M. & Astier, J. P. (2004). Temperature and pH effect on the polymorphism of aprotinin (BPTI) in sodium bromide solutions. Cryst. Growth Des. 4, 1137-1141.
    • (2004) Cryst. Growth Des. , vol.4 , pp. 1137-1141
    • Veesler, S.1    Ferte, N.2    Costes, M.S.3    Czjzek, M.4    Astier, J.P.5
  • 136
    • 77952078834 scopus 로고    scopus 로고
    • Acoustic matrix microseeding: Improving protein crystal growth with minimal chemical bias
    • Villasen? or, A. G. , Wong, A., Shao, A., Garg, A., Kuglstatter, A. & Harris, S. F. (2010). Acoustic matrix microseeding: improving protein crystal growth with minimal chemical bias. Acta Cryst. D66, 568-576.
    • (2010) Acta Cryst. , vol.D66 , pp. 568-576
    • Villasenor, A.G.1    Wong, A.2    Shao, A.3    Garg, A.4    Kuglstatter, A.5    Harris, S.F.6
  • 137
    • 0042863130 scopus 로고    scopus 로고
    • Solubility and crystallization of xylose isomerase from Streptomyces rubiginosus
    • Vuolanto, A., Uotila, S., Leisola, M. & Visuri, K. (2003). Solubility and crystallization of xylose isomerase from Streptomyces rubiginosus. J. Cryst. Growth, 257, 403-411.
    • (2003) J. Cryst. Growth , vol.257 , pp. 403-411
    • Vuolanto, A.1    Uotila, S.2    Leisola, M.3    Visuri, K.4
  • 138
    • 0014323026 scopus 로고
    • Micro diffusion cells for the growth of single protein crystals by means of equilibrium dialysis
    • Zeppezauer, M., Eklund, H. & Zeppezauer, E. S. ( 1968). Micro diffusion cells for the growth of single protein crystals by means of equilibrium dialysis. Arch. Biochem. Biophys. 126, 564-573.
    • (1968) Arch. Biochem. Biophys. , vol.126 , pp. 564-573
    • Zeppezauer, M.1    Eklund, H.2    Zeppezauer, E.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.