메뉴 건너뛰기




Volumn 29, Issue 3, 1996, Pages 227-278

Trends and challenges in experimental macromolecular crystallography

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 10544229793     PISSN: 00335835     EISSN: None     Source Type: Journal    
DOI: 10.1017/s0033583500005837     Document Type: Review
Times cited : (74)

References (214)
  • 1
    • 0026117802 scopus 로고
    • The effect of protein contaminants on the crystallisation of turkey egg white lysozyme
    • ABERGEL, C., NESA, M. P. & FONTECILLA-CAMPS, J. C. (1991). The effect of protein contaminants on the crystallisation of turkey egg white lysozyme. J. Cryst. Growth 110, 11-19.
    • (1991) J. Cryst. Growth , vol.110 , pp. 11-19
    • Abergel, C.1    Nesa, M.P.2    Fontecilla-Camps, J.C.3
  • 2
    • 0000050047 scopus 로고
    • Development of non-intensified charge-coupled device area X-ray detectors
    • ALLINSON, N. M. (1994). Development of non-intensified charge-coupled device area X-ray detectors. J. Synchrotron Rad. 1, 54-62.
    • (1994) J. Synchrotron Rad. , vol.1 , pp. 54-62
    • Allinson, N.M.1
  • 3
    • 0004304367 scopus 로고
    • High speed, high resolution data collection on spinach rubisco using a Weissenberg camera at the Photon Factory
    • Edited by Moras, D., Podjarny, A. D. & Thierry, J. C. Oxford University Press
    • ANDERSSON, I. A., CLIFTON, I. J., FULOP, V. & HAJDU, J. (1991). High speed, high resolution data collection on spinach rubisco using a Weissenberg camera at the Photon Factory. In Crystallographic Computing. Edited by Moras, D., Podjarny, A. D. & Thierry, J. C. Oxford University Press, p.20-28.
    • (1991) Crystallographic Computing , pp. 20-28
    • Andersson, I.A.1    Clifton, I.J.2    Fulop, V.3    Hajdu, J.4
  • 5
    • 84973021937 scopus 로고
    • Protein crystal growth: An approach based on phase diagram determination
    • ATAKA, M. (1993). Protein crystal growth: an approach based on phase diagram determination. Phase Transitions 45, 205-219.
    • (1993) Phase Transitions , vol.45 , pp. 205-219
    • Ataka, M.1
  • 6
    • 0024036988 scopus 로고
    • Systematic studies on the crystallisation of lysozyme. Determination and use of phase diagrams
    • ATAKA, M. & ASAI, M. (1988). Systematic studies on the crystallisation of lysozyme. Determination and use of phase diagrams. J. Cryst. Growth 90, 86-93.
    • (1988) J. Cryst. Growth , vol.90 , pp. 86-93
    • Ataka, M.1    Asai, M.2
  • 7
    • 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
  • 8
    • 10544236956 scopus 로고    scopus 로고
    • Increasing the number of crystallisation conditions by using microbatch screening
    • Proceedings of the Sixth International Conference on Crystallisation of Biological Macromolecules. in press
    • BALDOCK, P., MILLS, V. & SHAW STEWART, P. D. (1996). Increasing the number of crystallisation conditions by using microbatch screening. Proceedings of the Sixth International Conference on Crystallisation of Biological Macromolecules. J. Crystal Growth, in press.
    • (1996) J. Crystal Growth
    • Baldock, P.1    Mills, V.2    Shaw Stewart, P.D.3
  • 9
    • 0039126748 scopus 로고
    • Accuracy in Laue X-ray diffraction analysis of protein structure
    • BARTUNIK, H. D., BARTSCH, H. H. & QUICHEN, H. (1992). Accuracy in Laue X-ray diffraction analysis of protein structure. Acta Cryst. A 48, 180-188.
    • (1992) Acta Cryst. A , vol.48 , pp. 180-188
    • Bartunik, H.D.1    Bartsch, H.H.2    Quichen, H.3
  • 10
    • 4243503763 scopus 로고
    • A gel-mediated feeding technique for protein crystal growth from hanging drops
    • BERNARD, Y., DEGOY, S., LEFAUCHEUX, F. & ROBERT, M. C. (1994). A gel-mediated feeding technique for protein crystal growth from hanging drops. Acta Cryst. D 50, 504-507.
    • (1994) Acta Cryst. D , vol.50 , pp. 504-507
    • Bernard, Y.1    Degoy, S.2    Lefaucheux, F.3    Robert, M.C.4
  • 11
    • 0028659872 scopus 로고
    • Analysis of transient structures by cryo-microscopy combined with rapid measuring of spray droplets
    • BERRIMAN, J. & UNWIN, N. (1994). Analysis of transient structures by cryo-microscopy combined with rapid measuring of spray droplets. Ultramicroscopy 56, 241-252.
    • (1994) Ultramicroscopy , vol.56 , pp. 241-252
    • Berriman, J.1    Unwin, N.2
  • 15
    • 10544249909 scopus 로고    scopus 로고
    • (1993). UK patent GB 2 249 492 B on 'Crystallisation of Materials'; filed 13/12/89, published 13/10/93
    • BLOW, D. M., SHAW STEWART, P. D. & MAEDER, D. (1993). UK patent GB 2 249 492 B on 'Crystallisation of Materials'; filed 13/12/89, published 13/10/93.
    • Blow, D.M.1    Shaw Stewart, P.D.2    Maeder, D.3
  • 18
    • 0027109282 scopus 로고
    • Experimental equipment for protein crystallisation in microgravity facilities
    • BOSCH, R., LAUTENSCHLAGER, P., POTTHAST, L. & STAPELMANN, J. (1992). Experimental equipment for protein crystallisation in microgravity facilities. J. Cryst. Growth 122, 310-316.
    • (1992) J. Cryst. Growth , vol.122 , pp. 310-316
    • Bosch, R.1    Lautenschlager, P.2    Potthast, L.3    Stapelmann, J.4
  • 21
    • 0024082384 scopus 로고
    • A new protein crystallography station on the SRS Wiggler beamline for very rapid Laue and rapidly tunable monochromatic experiments: I. Design Principles, Ray Tracing and Heat calculations
    • BRAMMER, R. C., HELLIWELL, J. R., LAMB, W., LILJAS, A., MOORE, P. R., THOMPSON, A. W. & RATHBONE, K. (1988). A new protein crystallography station on the SRS Wiggler beamline for very rapid Laue and rapidly tunable monochromatic experiments: I. Design Principles, Ray Tracing and Heat calculations. Nucl. Instrum. & Methods A271, 678-687.
    • (1988) Nucl. Instrum. & Methods , vol.A271 , pp. 678-687
    • Brammer, R.C.1    Helliwell, J.R.2    Lamb, W.3    Liljas, A.4    Moore, P.R.5    Thompson, A.W.6    Rathbone, K.7
  • 22
    • 4243898009 scopus 로고
    • Poly(ethylene) glycol monomethyl ethers - An alternative to poly(ethylene) glycols in protein crystallisation
    • BRZOZOWSKI, A. M. & TOLLEY, S. P. (1994). Poly(ethylene) glycol monomethyl ethers - an alternative to poly(ethylene) glycols in protein crystallisation. Acta Cryst. D 50, 466-468.
    • (1994) Acta Cryst. D , vol.50 , pp. 466-468
    • Brzozowski, A.M.1    Tolley, S.P.2
  • 25
    • 0002865772 scopus 로고
    • Efficient factorial designs and the analysis of macromolecular crystal growth conditions
    • CARTER, C. W. JR. (1990). Efficient factorial designs and the analysis of macromolecular crystal growth conditions. Methods: a companion to Methods in Enzymology. 1, 12-24.
    • (1990) Methods: A Companion to Methods in Enzymology , vol.1 , pp. 12-24
    • Carter Jr., C.W.1
  • 26
    • 0002944634 scopus 로고
    • Design of crystallisation experiments and protocols
    • edited by Ducruix, A & Giegé, R, IRL Press at Oxford University Press
    • CARTER, C. W. JR. (1992). Design of crystallisation experiments and protocols. In Crystallisation of Nucleic Acids and Proteins. A Practical Approach, edited by Ducruix, A & Giegé, R, pp 47-71. IRL Press at Oxford University Press.
    • (1992) Crystallisation of Nucleic Acids and Proteins. A Practical Approach , pp. 47-71
    • Carter Jr., C.W.1
  • 27
    • 0018787717 scopus 로고
    • Protein crystallisation using incomplete factorial experiments
    • CARTER, C. W. JR. & CARTER C. W. (1979). Protein crystallisation 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
  • 28
    • 0027109324 scopus 로고
    • Laser scattering in a hanging drop vapour diffusion apparatus for protein crystal growth in a microgravity environment
    • CASAY, G. A. & WILSON, W. W. (1992). Laser scattering in a hanging drop vapour diffusion apparatus for protein crystal growth in a microgravity environment. J. Cryst. Growth 122, 95-101.
    • (1992) J. Cryst. Growth , vol.122 , pp. 95-101
    • Casay, G.A.1    Wilson, W.W.2
  • 30
    • 0029633120 scopus 로고
    • Microgravity protein crystallisation aboard the Photon satellite
    • CHAYEN, N. E. (1995). Microgravity protein crystallisation aboard the Photon satellite. J. Cryst. Growth 153, 175-179.
    • (1995) J. Cryst. Growth , vol.153 , pp. 175-179
    • Chayen, N.E.1
  • 31
    • 0029995709 scopus 로고    scopus 로고
    • A novel technique for container less protein crystallisation
    • in press
    • CHAYEN, N. E. (1996). A novel technique for container less protein crystallisation. Protein Engineering, in press.
    • (1996) Protein Engineering
    • Chayen, N.E.1
  • 32
    • 0024036036 scopus 로고
    • Solubility of glucose isomerase in ammonium sulphate solutions
    • CHAYEN, N. E., 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.E.1    Akins, J.2    Campbell-Smith, S.3    Blow, D.M.4
  • 33
    • 0024733041 scopus 로고
    • Trigonal glucose isomerase crystals require thymol for their growth and stability
    • CHAYEN, N. E., LLOYD, L., COLLYER, C. A. & BLOW, D. M. (1989). Trigonal glucose isomerase crystals require thymol for their growth and stability. J. Cryst. Growth 97, 367-374.
    • (1989) J. Cryst. Growth , vol.97 , pp. 367-374
    • Chayen, N.E.1    Lloyd, L.2    Collyer, C.A.3    Blow, D.M.4
  • 34
    • 0000192748 scopus 로고
    • An automated system for microbatch protein crystallisation and screening
    • CHAYEN, N. E., SHAW STEWART, P. D., MAEDER, D. L. & BLOW, D. M. (1990). An automated system for microbatch protein crystallisation 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
  • 35
    • 0027109260 scopus 로고
    • Microbatch crystallisation under oil - A new technique allowing many small-volume crystallisation trials
    • CHAYEN, N. E., SHAW STEWART, P. D. & BLOW, D. M. (1992). Microbatch crystallisation under oil - a new technique allowing many small-volume crystallisation 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
  • 36
    • 0027530394 scopus 로고
    • Control of nucleation in the crystallisation of lysozyme
    • CHAYEN, N. E., RADCLIFFE, J. & BLOW, D. M. (1993). Control of nucleation in the crystallisation of lysozyme. Protein Science 2, 113-118.
    • (1993) Protein Science , vol.2 , pp. 113-118
    • Chayen, N.E.1    Radcliffe, J.2    Blow, D.M.3
  • 37
    • 0003026698 scopus 로고
    • New developments of the IMPAX small-volume crystallisation system
    • CHAYEN, N. E., SHAW STEWART, P. D. & BALDOCK, P. (1994). New developments of the IMPAX small-volume crystallisation system. Acta Cryst. D 50, 456-458.
    • (1994) Acta Cryst. D , vol.50 , pp. 456-458
    • Chayen, N.E.1    Shaw Stewart, P.D.2    Baldock, P.3
  • 41
    • 0001828476 scopus 로고
    • Growth of KDP crystals from solution
    • Editors: Givargizov, E. I. & Grinberg, S. A. Consultants Bureau, NY, London
    • CHERNOV, A. A., RASHKOVICH, L. N., SMOL'SKII, I. L., KUZNETSOV, Y. G., MKRTCHYAN, A. A. & MALKIN, A. I. (1988). Growth of KDP crystals from solution. In Growth of Crystals. Editors: Givargizov, E. I. & Grinberg, S. A. Vol. 15, pp 43-91. Consultants Bureau, NY, London.
    • (1988) Growth of Crystals , vol.15 , pp. 43-91
    • Chernov, A.A.1    Rashkovich, L.N.2    Smol'skii, I.L.3    Kuznetsov, Y.G.4    Mkrtchyan, A.A.5    Malkin, A.I.6
  • 42
    • 0000449646 scopus 로고
    • Improvement of macromolecular electron density maps by the simultaneous application of real and reciprocal space constraints
    • COWTAN, K. D. & MAIN, P. (1993). Improvement of macromolecular electron density maps by the simultaneous application of real and reciprocal space constraints. Acta Cryst. D 49, 148-157.
    • (1993) Acta Cryst. D , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 43
    • 85055694230 scopus 로고
    • Experiments with automated protein crystallisation
    • COX, M. J. & WEBER, P. C. (1987). Experiments with automated protein crystallisation. J. Appl. Cryst. 20, 366-373.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 366-373
    • Cox, M.J.1    Weber, P.C.2
  • 44
    • 84944818485 scopus 로고
    • Multiplicity Distribution of Reflections in Laue Diffraction
    • CRUICKSHANK, D. W. J., HELLIWELL, J. R. & MOFFAT, K. (1987). Multiplicity Distribution of Reflections in Laue Diffraction. Acta. Cryst. A 43, 656-674.
    • (1987) Acta. Cryst. A , vol.43 , pp. 656-674
    • Cruickshank, D.W.J.1    Helliwell, J.R.2    Moffat, K.3
  • 45
    • 0000578877 scopus 로고
    • Angular distribution of reflections in Laue diffraction
    • CRUICKSHANK, D. W. J., HELLIWELL, J. R. & MOFFAT, K. (1991). Angular distribution of reflections in Laue diffraction. Acta Cryst. A 47, 352-373.
    • (1991) Acta Cryst. A , vol.47 , pp. 352-373
    • Cruickshank, D.W.J.1    Helliwell, J.R.2    Moffat, K.3
  • 47
    • 0003087471 scopus 로고
    • Screening and optimization strategies for macromolecular crystal growth
    • CUDNEY, R., PATEL, S., WEISGRABER, K., NEWHOUSE, Y. & MCPHERSON, A. (1994a). Screening and optimization strategies for macromolecular crystal growth. Acta Cryst. D 50, 414-423.
    • (1994) Acta Cryst. D , vol.50 , pp. 414-423
    • Cudney, R.1    Patel, S.2    Weisgraber, K.3    Newhouse, Y.4    Mcpherson, A.5
  • 48
    • 0000007040 scopus 로고
    • Crystallisation of macromolecules in silica gels
    • CUDNEY, B., PATEL, S. & MCPHERSON, A. (1994b). Crystallisation of macromolecules in silica gels. Acta Cryst. D 50, 479-483.
    • (1994) Acta Cryst. D , vol.50 , pp. 479-483
    • Cudney, B.1    Patel, S.2    Mcpherson, A.3
  • 49
    • 0030565935 scopus 로고    scopus 로고
    • A novel approach to crystallising proteins under oil
    • Proceedings of the Sixth International Conference on Crystallisation of Biological Macromolecules. in press
    • D'ARCY, A., ELMORE, C., STIHLE, M. & JOHNSTON, J. E. (1996). A novel approach to crystallising proteins under oil. Proceedings of the Sixth International Conference on Crystallisation of Biological Macromolecules. J. Cryst. Growth, in press.
    • (1996) J. Cryst. Growth
    • D'arcy, A.1    Elmore, C.2    Stihle, M.3    Johnston, J.E.4
  • 50
    • 0000485891 scopus 로고
    • The reflection of X-rays from imperfect crystals
    • DARWIN, C. G. (1922). The reflection of X-rays from imperfect crystals. Phil. Mag. 43, 800-829.
    • (1922) Phil. Mag. , vol.43 , pp. 800-829
    • Darwin, C.G.1
  • 54
    • 0026119323 scopus 로고
    • The solubility dependence of canavalin on pH and temperature
    • DEMATTEI, R. C. & FEIGELSON, R. S. (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
    • Demattei, R.C.1    Feigelson, R.S.2
  • 55
    • 0011168698 scopus 로고
    • Greatly reduced radiation damage in ribonuclease crystals mounted on glass fibres
    • DEWAN, J. C. & TILTON, R. F. (1987). Greatly reduced radiation damage in ribonuclease crystals mounted on glass fibres. J. Appl. Cryst. 20, 130-132.
    • (1987) J. Appl. Cryst. , vol.20 , pp. 130-132
    • Dewan, J.C.1    Tilton, R.F.2
  • 58
    • 0027431196 scopus 로고
    • Synchrotron beamlines for macromolecular crystallography
    • EALICK, S. & WALTER R. (1993). Synchrotron beamlines for macromolecular crystallography. Current Opinion in Structural Biology 3, 725-736.
    • (1993) Current Opinion in Structural Biology , vol.3 , pp. 725-736
    • Ealick, S.1    Walter, R.2
  • 59
    • 0343374919 scopus 로고    scopus 로고
    • A removable arc for mounting and recovering flash-cooled crystals
    • ENGEL, C., WIERENGA, R. & TUCKER, P. A. (1996). A removable arc for mounting and recovering flash-cooled crystals. J. Appl Crystallogr. 29, 208-210.
    • (1996) J. Appl Crystallogr. , vol.29 , pp. 208-210
    • Engel, C.1    Wierenga, R.2    Tucker, P.A.3
  • 60
    • 0000488635 scopus 로고
    • Orthorhombic lysozyme solubility
    • EWING, F., FORSYTHE, E., & PUSEY, M. (1994). Orthorhombic lysozyme solubility. Acta Cryst. D 50, 424-428.
    • (1994) Acta Cryst. D , vol.50 , pp. 424-428
    • Ewing, F.1    Forsythe, E.2    Pusey, M.3
  • 61
    • 0027109270 scopus 로고
    • Controlling nucleation in protein solutions
    • FEIGELSON, R. S. & DEMATTEI, R. C. (1992). Controlling nucleation in protein solutions. J. Cryst. Growth 122, 21-30.
    • (1992) J. Cryst. Growth , vol.122 , pp. 21-30
    • Feigelson, R.S.1    Demattei, R.C.2
  • 62
    • 0001553126 scopus 로고
    • The perfection of protein crystals probed by direct recording of Bragg reflection profiles with a quasiplanar X-ray wave
    • FOURME, R., DUCRUIX, A., RIESS-KAUTT, M. & CAPELLE, B. (1995). The perfection of protein crystals probed by direct recording of Bragg reflection profiles with a quasiplanar X-ray wave. J. Synchrotron Rad. 2, 136-142.
    • (1995) J. Synchrotron Rad. , vol.2 , pp. 136-142
    • Fourme, R.1    Ducruix, A.2    Riess-Kautt, M.3    Capelle, B.4
  • 63
    • 0343699286 scopus 로고
    • Some practical details on data collection at 100 K in Data collection and Processing
    • Compiled by Sawyer, L., Isaacs, N. & Bailey, S.
    • GAMBLIN, S. J. & RODGERS, D. W. (1993). Some practical details on data collection at 100 K in Data collection and Processing. Proceedings of the Daresbury CCP4 study weekend. 28-32. Compiled by Sawyer, L., Isaacs, N. & Bailey, S.
    • (1993) Proceedings of the Daresbury CCP4 Study Weekend , pp. 28-32
    • Gamblin, S.J.1    Rodgers, D.W.2
  • 64
    • 0000064890 scopus 로고
    • Investigations on protein crystal growth by the gel acupuncture method
    • GARCIA-RUIZ, J. M. & MORENO, A. (1994). Investigations on protein crystal growth by the gel acupuncture method. Acta Cryst. D 50, 484-490.
    • (1994) Acta Cryst. D , vol.50 , pp. 484-490
    • Garcia-Ruiz, J.M.1    Moreno, A.2
  • 65
    • 0000898340 scopus 로고
    • Biological macromolecule crystallisation 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 crystallisation database, version 3.0: New features, data and the NASA archive for protein crystal growth data. Acta Cryst. D 50, 408-413.
    • (1994) Acta Cryst. D , vol.50 , pp. 408-413
    • Gilliland, G.L.1    Tung, M.2    Blakeslee, D.M.3    Ladner, J.E.4
  • 66
    • 0028001874 scopus 로고
    • Data collection at short wavelengths in protein crystallography
    • GONZALEZ, A., DENNY, R. & NAVE, C. (1994). Data collection at short wavelengths in protein crystallography. Acta Cryst. D 50, 276-282.
    • (1994) Acta Cryst. D , vol.50 , pp. 276-282
    • Gonzalez, A.1    Denny, R.2    Nave, C.3
  • 67
    • 0001387283 scopus 로고
    • Oscillation camera data processing; Reflecting range and prediction of partiality I. Conventional X-ray sources
    • GREENHOUGH, T. J. & HELLIWELL, J. R. (1982). Oscillation camera data processing; Reflecting range and prediction of partiality I. Conventional X-ray sources. J. Appl. Cryst. 15, 338-351
    • (1982) J. Appl. Cryst. , vol.15 , pp. 338-351
    • Greenhough, T.J.1    Helliwell, J.R.2
  • 68
    • 0029643796 scopus 로고
    • Charge coupled device X-ray detectors for macromolecular crystallography
    • GRUNER, S. & EALICK, S. (1995). Charge coupled device X-ray detectors for macromolecular crystallography. Structure 3, 13-15.
    • (1995) Structure , vol.3 , pp. 13-15
    • Gruner, S.1    Ealick, S.2
  • 69
    • 0027728765 scopus 로고
    • A fast and portable microspectrophotometer for protein crystallography
    • HADFIELD, A. & HAJDU, J. (1993). A fast and portable microspectrophotometer for protein crystallography. J. Appl. Cryst. 26, 839-842.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 839-842
    • Hadfield, A.1    Hajdu, J.2
  • 72
    • 0027191459 scopus 로고
    • Fast X-ray crystallography and time-resolved structures
    • HAJDU, J. & ANDERSSON, I. (1993). Fast X-ray crystallography and time-resolved structures. Annu. Rev. Biophys. Biomol. Struct. 22, 467-498.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 467-498
    • Hajdu, J.1    Andersson, I.2
  • 74
    • 0029068918 scopus 로고
    • Silicon pixel detectors for X-ray diffraction studies with synchrotron radiation
    • HALL, G. (1995). Silicon pixel detectors for X-ray diffraction studies with synchrotron radiation. Quarterly Reviews of Biophysics 28(1), 1.
    • (1995) Quarterly Reviews of Biophysics , vol.28 , Issue.1 , pp. 1
    • Hall, G.1
  • 75
    • 0039126745 scopus 로고
    • Protein micro-crystal diffraction and the effects of radiation damage with ultra high flux synchrotron radiation
    • HEDMAN, B., HODGSON, K. O., HELLIWELL, J. R., LIDDINGTON, R. & PAPIZ, M. Z. (1985). Protein micro-crystal diffraction and the effects of radiation damage with ultra high flux synchrotron radiation. PNAS.USA 82, 7604-7607.
    • (1985) PNAS.USA , vol.82 , pp. 7604-7607
    • Hedman, B.1    Hodgson, K.O.2    Helliwell, J.R.3    Liddington, R.4    Papiz, M.Z.5
  • 76
    • 0039126830 scopus 로고
    • Optimisation of anomalous scattering and structural studies of proteins using synchrotron radiation
    • HELLIWELL, J. R. (1979). Optimisation of anomalous scattering and structural studies of proteins using synchrotron radiation. In Daresbury Study Weekend Proceedings DL/SCI.R13, p. 1-6.
    • (1979) Daresbury Study Weekend Proceedings DL/SCI.R13 , pp. 1-6
    • Helliwell, J.R.1
  • 77
    • 0019067695 scopus 로고
    • The use of electronic area detectors for synchrotron X-radiation protein crystallography with particular reference to the Daresbury SRS
    • HELLIWELL, J. R. (1982). The use of electronic area detectors for synchrotron X-radiation protein crystallography with particular reference to the Daresbury SRS. Nucl. Instrum. & Meths. 201, 153-174.
    • (1982) Nucl. Instrum. & Meths. , vol.201 , pp. 153-174
    • Helliwell, J.R.1
  • 78
    • 0001327635 scopus 로고
    • Synchrotron X-radiation protein crystallography: Instrumentation, methods and applications
    • HELLIWELL, J. R. (1984). Synchrotron X-radiation protein crystallography: instrumentation, methods and applications. Reports on Progress in Physics 47, 1403-1497.
    • (1984) Reports on Progress in Physics , vol.47 , pp. 1403-1497
    • Helliwell, J.R.1
  • 79
    • 0011723351 scopus 로고
    • Protein Crystallography with Synchrotron Radiation
    • HELLIWELL, J. R. (1985). Protein Crystallography with Synchrotron Radiation. J. Molec. Struct. 130, 63-91.
    • (1985) J. Molec. Struct. , vol.130 , pp. 63-91
    • Helliwell, J.R.1
  • 81
    • 0024037950 scopus 로고
    • Protein crystal perfection and the nature of radiation damage
    • HELLIWELL, J. R. (1988). Protein crystal perfection and the nature of radiation damage. J. Cryst. Growth 90, 250-272.
    • (1988) J. Cryst. Growth , vol.90 , pp. 250-272
    • Helliwell, J.R.1
  • 83
    • 0040078085 scopus 로고
    • Synchrotron X-ray crystallography techniques: Time-resolved aspects of data collection
    • HELLIWELL, J. R. (1992b). Synchrotron X-ray crystallography techniques: Time-resolved aspects of data collection. Phil. Trans. Roy. Soc. Lond. A 340, 221-232.
    • (1992) Phil. Trans. Roy. Soc. Lond. A , vol.340 , pp. 221-232
    • Helliwell, J.R.1
  • 84
    • 0010568193 scopus 로고
    • The choice of X-ray wavelength in macromolecular crystallography
    • DI/SCI/R34. Compiled by Sawyer, L., Isaacs, N. & Bailey, S.
    • HELLIWELL J. R. (1993). The choice of X-ray wavelength in macromolecular crystallography. Proceedings of the SERC Daresbury Study Weekend. DI/SCI/R34. Compiled by Sawyer, L., Isaacs, N. & Bailey, S., pp. 80-88.
    • (1993) Proceedings of the SERC Daresbury Study Weekend , pp. 80-88
    • Helliwell, J.R.1
  • 85
    • 0039719130 scopus 로고
    • The ESRF as a facility for protein crystallography: A report and design study
    • CERN, Geneva
    • HELLIWELL, J. R. & FOURME, R. (1983). The ESRF as a facility for protein crystallography: A report and design study. ESRP Report IRI-4/83, CERN, Geneva, pp. 1-36.
    • (1983) ESRP Report IRI-4/83 , pp. 1-36
    • Helliwell, J.R.1    Fourme, R.2
  • 86
    • 0010568917 scopus 로고    scopus 로고
    • X-ray crystallography in structural chemistry and molecular biology
    • Feature Article
    • HELLIWELL, J. R. & HELLIWELL, M. (1996). X-ray crystallography in structural chemistry and molecular biology. Feature Article, Chem. Comm., No. 14, 1595-1602.
    • (1996) Chem. Comm. , Issue.14 , pp. 1595-1602
    • Helliwell, J.R.1    Helliwell, M.2
  • 87
    • 0020449492 scopus 로고
    • Central data collection facility for protein crystallography, small angle diffraction and scattering at the Daresbury SRS
    • HELLIWELL, J. R., GREENHOUGH, T. J., CARR, P., RULE, S. A., MOORE, P. R., THOMPSON, A. W. & WORGAN, J. S. (1982). Central data collection facility for protein crystallography, small angle diffraction and scattering at the Daresbury SRS. J. Phys. E. 15, 1363-1372.
    • (1982) J. Phys. E. , vol.15 , pp. 1363-1372
    • Helliwell, J.R.1    Greenhough, T.J.2    Carr, P.3    Rule, S.A.4    Moore, P.R.5    Thompson, A.W.6    Worgan, J.S.7
  • 90
    • 0000581720 scopus 로고
    • An investigation of the perfection of lysozyme protein crysals grown in microgravity (Spacehab-1 and IML-2) and on earth
    • Springer Verlag Lecture Notes in Physics. Edited by Ratke, L., Walter, H. & Feuerbacher, B.
    • HELLIWELL, J. R., SNELL, E. H. & WEISGERBER, S. (1995). An investigation of the perfection of lysozyme protein crysals grown in microgravity (Spacehab-1 and IML-2) and on earth. Pages 155-170 in Proceedings of the Berlin Conference on Microgravity Research. Springer Verlag Lecture Notes in Physics. Edited by Ratke, L., Walter, H. & Feuerbacher, B.
    • (1995) Proceedings of the Berlin Conference on Microgravity Research , pp. 155-170
    • Helliwell, J.R.1    Snell, E.H.2    Weisgerber, S.3
  • 91
    • 0025071357 scopus 로고
    • Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction
    • HENDERSON, R. (1990). Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction. Proc. R. Soc. Lond. B 241, 6-8.
    • (1990) Proc. R. Soc. Lond. B , vol.241 , pp. 6-8
    • Henderson, R.1
  • 92
    • 0002735497 scopus 로고
    • Analysis of protein structure from diffraction measurements at multiple wavelengths
    • HENDRICKSON, W. (1985). Analysis of protein structure from diffraction measurements at multiple wavelengths. Trans. Americ. Cryst. Assoc. 21, 11-21.
    • (1985) Trans. Americ. Cryst. Assoc. , vol.21 , pp. 11-21
    • Hendrickson, W.1
  • 93
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • HENDRICKSON, W. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.1
  • 94
    • 0028807158 scopus 로고
    • The effects of filtration on protein nucleation in different growth media
    • HIRSCHLER, J., CHARON, M. H. & FONTECILLA-CAMPS, J. C. (1995). The effects of filtration on protein nucleation in different growth media. Protein Science 4, 2573-2577.
    • (1995) Protein Science , vol.4 , pp. 2573-2577
    • Hirschler, J.1    Charon, M.H.2    Fontecilla-Camps, J.C.3
  • 95
    • 84944510121 scopus 로고
    • Cryo-crystallography of biological macromolecules: A generally applicable method
    • HOPE, H. (1988). Cryo-crystallography of biological macromolecules: a generally applicable method. Acta Cryst. B 44, 22-26.
    • (1988) Acta Cryst. B , vol.44 , pp. 22-26
    • Hope, H.1
  • 96
    • 0025366965 scopus 로고
    • Crystallography of biological macromolecules at ultra-low temperature
    • HOPE, H. (1990). Crystallography of biological macromolecules at ultra-low temperature. Annu. Rev. Biophys., Biophys. Chem. 19, 107-126.
    • (1990) Annu. Rev. Biophys., Biophys. Chem. , vol.19 , pp. 107-126
    • Hope, H.1
  • 97
    • 10544249511 scopus 로고    scopus 로고
    • Personal communication
    • HOPE, H. (1996). Personal communication.
    • (1996)
    • Hope, H.1
  • 98
    • 0040311039 scopus 로고
    • The determination of phases of erythrocruorin using the two-wavelength method with iron as anomalous scatterer
    • Edited by Ramaseshan, S. & Abrahams, S. C., Copenhagen: Munksgaard
    • HOPPE, W. & JAKUBOWSKI, U. (1975). The determination of phases of erythrocruorin using the two-wavelength method with iron as anomalous scatterer. In Anomalous Scattering. Edited by Ramaseshan, S. & Abrahams, S. C., Copenhagen: Munksgaard, pp. 437-461.
    • (1975) Anomalous Scattering , pp. 437-461
    • Hoppe, W.1    Jakubowski, U.2
  • 100
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallisation of proteins
    • JANCARIK, J. & KIM, S. H. (1991). Sparse matrix sampling: a screening method for crystallisation of proteins. J. Appl. Cryst. 24, 409-411.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 101
    • 0348028833 scopus 로고
    • Anomalous scattering in X-ray diffraction and use of several wavelengths
    • KARLE, J. (1967). Anomalous scattering in X-ray diffraction and use of several wavelengths. Appl. Opt. 6, 2132-2135.
    • (1967) Appl. Opt. , vol.6 , pp. 2132-2135
    • Karle, J.1
  • 102
    • 84987108897 scopus 로고
    • Some developments in anomalous dispersion for the structural investigation of macromolecular systems in Biology
    • KARLE, J. (1980). Some developments in anomalous dispersion for the structural investigation of macromolecular systems in Biology. Int. J. Quantum Chem. Quantum Biol. Symp. 1, 357-367.
    • (1980) Int. J. Quantum Chem. Quantum Biol. Symp. , vol.1 , pp. 357-367
    • Karle, J.1
  • 103
    • 0000122663 scopus 로고
    • Search designs for protein crystallisation based on orthogonal arrays
    • KINGSTON, R. L., BAKER, H. M. & BAKER, E. N. (1994). Search designs for protein crystallisation based on orthogonal arrays. Acta Cryst. D 50, 429-440.
    • (1994) Acta Cryst. D , vol.50 , pp. 429-440
    • Kingston, R.L.1    Baker, H.M.2    Baker, E.N.3
  • 104
    • 0000579314 scopus 로고
    • Interferometric observation of the interfacial concentration gradient layers around a lysozyme crystal
    • KOMATSU, H., MIYASHITA, S. & SUZUKI, Y. (1993). Interferometric observation of the interfacial concentration gradient layers around a lysozyme crystal. Jpn. J. Appl. Phys. 32 Pt. 2, 1855-1857.
    • (1993) Jpn. J. Appl. Phys. , vol.32 , Issue.2 PART , pp. 1855-1857
    • Komatsu, H.1    Miyashita, S.2    Suzuki, Y.3
  • 106
    • 0026124205 scopus 로고
    • Protein crystal growth rates determined by time lapse microphotography
    • KOSZELAK, S., MARTIN, D., NG, J. & MCPHERSON, A. (1991). Protein crystal growth rates determined by time lapse microphotography J. Cryst. Growth 110, 177-181.
    • (1991) J. Cryst. Growth , vol.110 , pp. 177-181
    • Koszelak, S.1    Martin, D.2    Ng, J.3    Mcpherson, A.4
  • 107
    • 0029071556 scopus 로고
    • Protein and virus crystal growth on International Microgravity Laboratory-2
    • KOSZELAK, S., DAY, J., LEJA, C., CUBNEY, R. & MCPHERSON, A. (1995). Protein and virus crystal growth on International Microgravity Laboratory-2. Biophys. J. 69, 13-19.
    • (1995) Biophys. J. , vol.69 , pp. 13-19
    • Koszelak, S.1    Day, J.2    Leja, C.3    Cubney, R.4    Mcpherson, A.5
  • 108
    • 0029143892 scopus 로고
    • Interferometric studies of growth kinetics and surface morphology in macromolecular crystal growth: Canavalin, thaumatin and turnip yellow mosaic virus
    • KUZNETSOV, Y. G., MALKIN, A. J., GREENWOOD, A. & MCPHERSON, A. (1995). Interferometric studies of growth kinetics and surface morphology in macromolecular crystal growth: Canavalin, thaumatin and turnip yellow mosaic virus. J. Structural Biology 114, 184-196.
    • (1995) J. Structural Biology , vol.114 , pp. 184-196
    • Kuznetsov, Y.G.1    Malkin, A.J.2    Greenwood, A.3    Mcpherson, A.4
  • 109
    • 0030566060 scopus 로고    scopus 로고
    • In situ atomic force microscopy studies of protein and virus crystal growth mechanisms
    • in press
    • KUZNETSOV, Y. G., MALKIN, A. J., GLANTZ, W. & MCPHERSON, A. (1996). In situ atomic force microscopy studies of protein and virus crystal growth mechanisms. J. Cryst. Growth, in press.
    • (1996) J. Cryst. Growth
    • Kuznetsov, Y.G.1    Malkin, A.J.2    Glantz, W.3    Mcpherson, A.4
  • 110
    • 4244171734 scopus 로고
    • Mechanisms of protein crystal growth: An atomic force microscopy study of canavalin crystallization
    • LAND, T. A., MALKIN, A. J., KUZNETSOV, Y. G., MCPHERSON, A & DEYOREO, J. J. (1995). Mechanisms of protein crystal growth: An atomic force microscopy study of canavalin crystallization. Physical Review Letters Vol. 75, No. 14, 2774-2777.
    • (1995) Physical Review Letters , vol.75 , Issue.14 , pp. 2774-2777
    • Land, T.A.1    Malkin, A.J.2    Kuznetsov, Y.G.3    Mcpherson, A.4    Deyoreo, J.J.5
  • 111
    • 0002574380 scopus 로고
    • Multiwire gas proportional counters: Decrepit antiques or classic performers?
    • LEWIs, R. A. (1994). Multiwire gas proportional counters: decrepit antiques or classic performers? J. Synchrotron Rad. 1, 43-53.
    • (1994) J. Synchrotron Rad. , vol.1 , pp. 43-53
    • Lewis, R.A.1
  • 112
    • 0038892267 scopus 로고
    • The sensitivity of the Laue method to small structural changes: Binding studies of human carbonic anhydrase II (HCA II)
    • LINDAHL, M., LILJAS, A., HABASH, J., HARROP, S. J. & HELLIWELL, J. R. (1992). The sensitivity of the Laue method to small structural changes: binding studies of human carbonic anhydrase II (HCA II). Acta Cryst. B48, 281-285.
    • (1992) Acta Cryst. , vol.B48 , pp. 281-285
    • Lindahl, M.1    Liljas, A.2    Habash, J.3    Harrop, S.J.4    Helliwell, J.R.5
  • 113
    • 10544244221 scopus 로고
    • Protein crystal growth in microgravity. Review of large scale temperature induction method: Bovine insulin, human insulin and human alpha interferon
    • Sixth International Conference on Crystallisation of Biological Macromolecules, Hiroshima, Japan. in press
    • LONG, M. M., BISHOP, J. B., NAGABHUSHAN, T. L., REICHERT, P., SMITH, G. D. & DELUCAS, L. J. (1995). Protein crystal growth in microgravity. Review of large scale temperature induction method: bovine insulin, human insulin and human alpha interferon. Sixth International Conference on Crystallisation of Biological Macromolecules, Hiroshima, Japan. J. Cryst. Growth, in press.
    • (1995) J. Cryst. Growth
    • Long, M.M.1    Bishop, J.B.2    Nagabhushan, T.L.3    Reichert, P.4    Smith, G.D.5    Delucas, L.J.6
  • 114
    • 0030566093 scopus 로고    scopus 로고
    • Containerless protein crystallization in floating drops: Application to crystal growth monitoring under reduced nucleation conditions
    • Proceedings of the Sixth International Conference on Crystallisation of Biological Macromolecules. in press
    • LORBER, B. & GIEGÉ, R. (1996). Containerless protein crystallization in floating drops: application to crystal growth monitoring under reduced nucleation conditions. Proceedings of the Sixth International Conference on Crystallisation of Biological Macromolecules. J. Crystal Growth, in press.
    • (1996) J. Crystal Growth
    • Lorber, B.1    Giegé, R.2
  • 115
    • 0027560478 scopus 로고
    • The influence of impurities on protein crystallisation; the case of lysozyme
    • LORBER, B., SKOURI, M., MUNCH, J. P. & GIEGÉ R. (1993). The influence of impurities on protein crystallisation; the case of lysozyme. J. Cryst. Growth 128, 1203-1211.
    • (1993) J. Cryst. Growth , vol.128 , pp. 1203-1211
    • Lorber, B.1    Skouri, M.2    Munch, J.P.3    Giegé, R.4
  • 116
    • 0029756707 scopus 로고    scopus 로고
    • Effect of high hydrostatic pressure on nucleation and growth of protein crystals
    • LORBER, B., JENNER, G. & GIEGÉ, R. (1996). Effect of high hydrostatic pressure on nucleation and growth of protein crystals. J. Cryst. Growth 158, 103-117.
    • (1996) J. Cryst. Growth , vol.158 , pp. 103-117
    • Lorber, B.1    Jenner, G.2    Giegé, R.3
  • 117
    • 0009528256 scopus 로고
    • Studies of insulin crystals at low temperatures: Effects on mosaic character and radiation sensitivity
    • LOW, B. M., CHEN, C. C., BERGER, J. E., SINGMANN, L. & PLETCHER, J. F. (1966). Studies of insulin crystals at low temperatures: effects on mosaic character and radiation sensitivity. Proc. Natl. Acad. Sci. USA 56, 1746-1750.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 1746-1750
    • Low, B.M.1    Chen, C.C.2    Berger, J.E.3    Singmann, L.4    Pletcher, J.F.5
  • 118
    • 0027539866 scopus 로고
    • Crystallisation of satellite tobacco mosaic virus 1. nucleation phenomena
    • MALKIN, A. J., CHEUNG, J. & MCPHERSON, A. (1993). Crystallisation of satellite tobacco mosaic virus 1. nucleation phenomena. J. Cryst. Growth 126, 544-554.
    • (1993) J. Cryst. Growth , vol.126 , pp. 544-554
    • Malkin, A.J.1    Cheung, J.2    Mcpherson, A.3
  • 122
    • 0027109318 scopus 로고
    • Two approaches to the rapid screening of crystallisation conditons
    • MCPHERSON, A. (1992). Two approaches to the rapid screening of crystallisation conditons. J. Cryst. Growth 122, 161-167.
    • (1992) J. Cryst. Growth , vol.122 , pp. 161-167
    • Mcpherson, A.1
  • 123
    • 0027642971 scopus 로고
    • Virus and protein crystal growth on earth and in microgravity
    • MCPHERSON, A. (1993). Virus and protein crystal growth on earth and in microgravity. J. Phys. D. Appl. Phys. 26, B104-B112.
    • (1993) J. Phys. D. Appl. Phys. , vol.26
    • Mcpherson, A.1
  • 124
    • 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
    • Mcpherson, A.1
  • 125
    • 0000909155 scopus 로고
    • Heterogeneous and epitaxial nucleation of protein crystals on mineral surfaces
    • MCPHERSON, A. & SCHLICHTA, P. (1988). Heterogeneous and epitaxial nucleation of protein crystals on mineral surfaces. Science 239, 385-387.
    • (1988) Science , vol.239 , pp. 385-387
    • Mcpherson, A.1    Schlichta, P.2
  • 126
    • 0029645277 scopus 로고
    • The science of macromolecular crystallisation
    • MCPHERSON, A., MALKIN, A. J. & KUZNETSOV, Y. G. (1995). The science of macromolecular crystallisation. Structure 3, 759-768.
    • (1995) Structure , vol.3 , pp. 759-768
    • Mcpherson, A.1    Malkin, A.J.2    Kuznetsov, Y.G.3
  • 127
    • 0024737404 scopus 로고
    • Phase diagram of a crystalline protein: Determination of the solubility of concanavalin A by a microquantitation assay
    • MIKOL, V. & GIEGÉ, 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    Giegé, R.2
  • 128
    • 0001857002 scopus 로고
    • The physical chemistry of protein crystallisation
    • edited by Ducruix, A. & Giegéy R., IRL Press at Oxford University Press
    • MIKOL, V. & GIEGÉ, R. (1992). The physical chemistry of protein crystallisation. In Crystallisation of Nucleic Acids and Proteins. A Practical Approach, edited by Ducruix, A. & Giegéy R., pp 219-239. IRL Press at Oxford University Press.
    • (1992) Crystallisation of Nucleic Acids and Proteins. A Practical Approach , pp. 219-239
    • Mikol, V.1    Giegé, R.2
  • 129
    • 0013132976 scopus 로고
    • Monitoring protein crystallisation by dynamic light scattering
    • MIKOL, V., HIRSCH, E. & GIEGE, R. (1989). Monitoring protein crystallisation by dynamic light scattering. FEBS Letters 258, 63-66.
    • (1989) FEBS Letters , vol.258 , pp. 63-66
    • Mikol, V.1    Hirsch, E.2    Giege, R.3
  • 130
    • 0028757855 scopus 로고
    • Flash freezing of protein crystals: Investigation of mosaic spread and diffraction limit with variation of cryoprotectant concentration
    • MITCHELL, E. P. & GARMAN, E. F. (1994). Flash freezing of protein crystals: investigation of mosaic spread and diffraction limit with variation of cryoprotectant concentration. J. Appl. Cryst. 27, 1070-1074.
    • (1994) J. Appl. Cryst. , vol.27 , pp. 1070-1074
    • Mitchell, E.P.1    Garman, E.F.2
  • 131
    • 0028761406 scopus 로고
    • Observation of the concentration distribution around a growing lysozyme crystal
    • MIYASHITA, S., KOMATSU, H., SUZUKI, Y. & NAKADA, T. (1994). Observation of the concentration distribution around a growing lysozyme crystal. J. Cryst. Growth 141, 419-424.
    • (1994) J. Cryst. Growth , vol.141 , pp. 419-424
    • Miyashita, S.1    Komatsu, H.2    Suzuki, Y.3    Nakada, T.4
  • 133
    • 0001204409 scopus 로고
    • X-ray Laue diffraction from protein crystals
    • MOFFAT, K., SZEBENYI, D. M. & BILDERBACK, D. (1984). X-ray Laue diffraction from protein crystals. Science 223, 1423-1425.
    • (1984) Science , vol.223 , pp. 1423-1425
    • Moffat, K.1    Szebenyi, D.M.2    Bilderback, D.3
  • 135
    • 0028498360 scopus 로고
    • High-speed acquisition system for Laue diffraction patterns
    • MOON, K. J., ALLINSON, N. M. & HELLIWELL, J. R. (1994). High-speed acquisition system for Laue diffraction patterns. Nucl. Instrum. & Meths. A348, 631-634.
    • (1994) Nucl. Instrum. & Meths. , vol.A348 , pp. 631-634
    • Moon, K.J.1    Allinson, N.M.2    Helliwell, J.R.3
  • 136
    • 84987357685 scopus 로고
    • A kinetic analysis of the reaction catalysed by (Hydroxymethyl) bilane synthase
    • NIEMANN, A. C., MATZINGER, P. K. & HAEDENER, A. (1994). A kinetic analysis of the reaction catalysed by (Hydroxymethyl) bilane synthase. Helvetica Chimica Acta 77, 1791-1809.
    • (1994) Helvetica Chimica Acta , vol.77 , pp. 1791-1809
    • Niemann, A.C.1    Matzinger, P.K.2    Haedener, A.3
  • 137
    • 0028413816 scopus 로고
    • Small angle neutron scattering from lysozyme in unsaturated solutions, to characterise the precrystallisation process
    • NIIMURA, N., MINEZAKI, Y., ATAKA, M. & KATSURA, T. (1994). Small angle neutron scattering from lysozyme in unsaturated solutions, to characterise the precrystallisation process. J. Cryst. Growth 137, 671-675.
    • (1994) J. Cryst. Growth , vol.137 , pp. 671-675
    • Niimura, N.1    Minezaki, Y.2    Ataka, M.3    Katsura, T.4
  • 138
    • 0029376213 scopus 로고
    • Aggregation in supersaturated lysozyme solution studied by time-resolved small angle neutron scattering
    • NIIMURA, N., MINEZAKI, Y., ATAKA, M. & KATSURA, T. (1995). Aggregation in supersaturated lysozyme solution studied by time-resolved small angle neutron scattering. J. Cryst. Growth 154, 136-144.
    • (1995) J. Cryst. Growth , vol.154 , pp. 136-144
    • Niimura, N.1    Minezaki, Y.2    Ataka, M.3    Katsura, T.4
  • 139
    • 0029650654 scopus 로고
    • Search for better crystals explores inner, outer space
    • NORMILE, D. (1995). Search for better crystals explores inner, outer space. Science 270, 1921-1992.
    • (1995) Science , vol.270 , pp. 1921-1992
    • Normile, D.1
  • 140
    • 0000305934 scopus 로고
    • Phase diagram determination to elucidate the crystal growth of the photoreaction center from Rhodobacter sphaeroides
    • ODAHARA, T., ATAKA, M. & KATSURA, T. (1994). Phase diagram determination to elucidate the crystal growth of the photoreaction center from Rhodobacter sphaeroides. Acta Cryst. D 50, 639-642.
    • (1994) Acta Cryst. D , vol.50 , pp. 639-642
    • Odahara, T.1    Ataka, M.2    Katsura, T.3
  • 141
    • 0001429250 scopus 로고
    • Determination of crystal structures by means of anomalously scattered X-rays
    • OKAYA, Y. & PEPINSKY, R. (1956). Determination of crystal structures by means of anomalously scattered X-rays. Phys. Rev. 103, 1645-1647.
    • (1956) Phys. Rev. , vol.103 , pp. 1645-1647
    • Okaya, Y.1    Pepinsky, R.2
  • 142
    • 0026172472 scopus 로고
    • A flexible approach to automated protein crystallisation
    • OLDFIELD, T. J., CESKA, T. A. & BRADY, R. L. (1991). A flexible approach to automated protein crystallisation. J. Appl. Cryst. 24, 255-260.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 255-260
    • Oldfield, T.J.1    Ceska, T.A.2    Brady, R.L.3
  • 143
    • 0027576544 scopus 로고
    • Application of real time phase shift interferometer to the measurement of concentration field
    • ONUMA, K., TSUKAMOTO, T. & NAKADATE, S. (1993). Application of real time phase shift interferometer to the measurement of concentration field. J. Cryst. Growth 129, 706-718.
    • (1993) J. Cryst. Growth , vol.129 , pp. 706-718
    • Onuma, K.1    Tsukamoto, T.2    Nakadate, S.3
  • 144
    • 0028809374 scopus 로고
    • Polymeric precipitants for the crystallisation of macromolecules
    • PATEL, S., CUDNEY, B. & MCPHERSON, A. (1995). Polymeric precipitants for the crystallisation of macromolecules. Biochem. Biophys. Res. Commun. 207, 819-828.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 819-828
    • Patel, S.1    Cudney, B.2    Mcpherson, A.3
  • 146
    • 0016853253 scopus 로고
    • Protein crystallography at sub-zero temperatures: Cryo-protective mother liquors for protein crystals
    • PETSKO, G. A. (1975). Protein crystallography at sub-zero temperatures: cryo-protective mother liquors for protein crystals. J. Mol. Biol. 96, 381-392.
    • (1975) J. Mol. Biol. , vol.96 , pp. 381-392
    • Petsko, G.A.1
  • 148
    • 10544232655 scopus 로고
    • Personal Communication
    • PHILLIPS, D. C. (1974). Personal Communication.
    • (1974)
    • Phillips, D.C.1
  • 149
    • 0029403885 scopus 로고
    • Crystal growth of lysozymes in media contaminated by parent molecules: Influence of gelled media
    • PROVOST, K. & ROBERT, M. C. (1995). Crystal growth of lysozymes in media contaminated by parent molecules: influence of gelled media. J. Cryst. Growth 156, 112-120.
    • (1995) J. Cryst. Growth , vol.156 , pp. 112-120
    • Provost, K.1    Robert, M.C.2
  • 150
    • 0000127614 scopus 로고
    • A double cell for controlling nucleation and growth of protein crystals
    • PRYZBYLSKA, M. (1989). A double cell for controlling nucleation and growth of protein crystals. J. Appl. Cryst. 22, 115-118.
    • (1989) J. Appl. Cryst. , vol.22 , pp. 115-118
    • Pryzbylska, M.1
  • 151
    • 0026124457 scopus 로고
    • Estimation of the initial equlibrium constants in the formation of tetragonal lysozyme nuclei
    • PUSEY, M. L. (1991). Estimation of the initial equlibrium constants in the formation of tetragonal lysozyme nuclei. J. Cryst. Growth, 110, 60-65.
    • (1991) J. Cryst. Growth , vol.110 , pp. 60-65
    • Pusey, M.L.1
  • 152
    • 0004261380 scopus 로고
    • A method for rapid liquid-solid phase solubility measurements using the protein lysozyme
    • PUSEY, M. L. & GERNERT, K. (1988). A method for rapid liquid-solid phase solubility measurements using the protein lysozyme. J. Cryst. Growth 88, 419-424.
    • (1988) J. Cryst. Growth , vol.88 , pp. 419-424
    • Pusey, M.L.1    Gernert, K.2
  • 153
    • 0026225252 scopus 로고
    • Micro-apparatus for rapid determinations of protein solubilities
    • PUSEY, M. L. & MUNSON, S. (1991). Micro-apparatus for rapid determinations of protein solubilities. J. Cryst. Growth 113, 385-389.
    • (1991) J. Cryst. Growth , vol.113 , pp. 385-389
    • Pusey, M.L.1    Munson, S.2
  • 154
    • 0008285604 scopus 로고
    • Laue crystallography for studying rapid reactions
    • REN, Z. & MOFFAT, K. (1994). Laue crystallography for studying rapid reactions. J. Synchrotron Rad. 1, 78-82.
    • (1994) J. Synchrotron Rad. , vol.1 , pp. 78-82
    • Ren, Z.1    Moffat, K.2
  • 155
    • 0000499436 scopus 로고
    • Quantitative analysis of synchrotron Laue diffraction patterns in macromolecular crystallography
    • REN, Z. & MOFFAT, K. (1995a). Quantitative analysis of synchrotron Laue diffraction patterns in macromolecular crystallography. J. Appl. Cryst. 28, 461-481.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 461-481
    • Ren, Z.1    Moffat, K.2
  • 156
    • 0001177107 scopus 로고
    • Deconvolution of energy overlaps in Laue diffraction
    • REN, Z. & MOFFAT, K. (1995b). Deconvolution of energy overlaps in Laue diffraction. J. Appl. Cryst. 28, 482-493.
    • (1995) J. Appl. Cryst. , vol.28 , pp. 482-493
    • Ren, Z.1    Moffat, K.2
  • 157
    • 0000659189 scopus 로고
    • Crystallisation of membrane proteins
    • edited by Ducruix, A. & Giegé, R., IRL Press at Oxford University Press
    • RIESS-HUSSON, F. (1992). Crystallisation of membrane proteins. In Crystallisation of Nucleic Acids and Proteins. A Practical Approach, edited by Ducruix, A. & Giegé, R., pp 175-193. IRL Press at Oxford University Press.
    • (1992) Crystallisation of Nucleic Acids and Proteins. A Practical Approach , pp. 175-193
    • Riess-Husson, F.1
  • 159
    • 0024035862 scopus 로고
    • Crystal growth in gels: Principles and applications
    • ROBERT, M. C. & LEFAUCHEUX, F. (1988). Crystal growth in gels: principles and applications. J. Cryst. Growth 90, 358-367.
    • (1988) J. Cryst. Growth , vol.90 , pp. 358-367
    • Robert, M.C.1    Lefaucheux, F.2
  • 161
    • 0028774714 scopus 로고
    • Cryocrystallography
    • RODGERS, D. (1994). Cryocrystallography. Structure, Vol 2. No. 12, 1135-1140.
    • (1994) Structure , vol.2 , Issue.12 , pp. 1135-1140
    • Rodgers, D.1
  • 162
    • 0030566049 scopus 로고    scopus 로고
    • Nucleation and crystallisation of globular proteins - What do we know and what is missing?
    • in press
    • ROSENBERGER (1996). Nucleation and crystallisation of globular proteins - what do we know and what is missing?. J. Cryst. Growth, in press.
    • (1996) J. Cryst. Growth
    • Rosenberger1
  • 163
    • 0027904939 scopus 로고
    • Temperature dependence of protein solubility - Determination and application to crystallisation 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 crystallisation in X-ray capillaries. J. Cryst. Growth 129, 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
  • 164
    • 0026124206 scopus 로고
    • Minimal intervention robotic protein crystallisation
    • RUBIN, B., TALATOUS, J. & LARSON, D. (1991). Minimal intervention robotic protein crystallisation. J. Cryst. Growth 110, 156-163.
    • (1991) J. Cryst. Growth , vol.110 , pp. 156-163
    • Rubin, B.1    Talatous, J.2    Larson, D.3
  • 165
    • 10544231493 scopus 로고
    • Atomic resolution cryocrystallography: BPTI and concanavalin A
    • Montreal
    • RUPP, B., HOPE, H. & PARKIN, S. (1995). Atomic resolution cryocrystallography: BPTI and concanavalin A. Abstract MO44 ACA Meeting, Montreal.
    • (1995) Abstract MO44 ACA Meeting
    • Rupp, B.1    Hope, H.2    Parkin, S.3
  • 166
    • 0028486181 scopus 로고
    • TAOS: An automatic system for protein crystallisation
    • SADAOUI, N., JANIN, J. & LEWIT-BENTLY, A. (1994). TAOS: an automatic system for protein crystallisation. J. Appl. Cryst. 27, 622-626.
    • (1994) J. Appl. Cryst. , vol.27 , pp. 622-626
    • Sadaoui, N.1    Janin, J.2    Lewit-Bently, A.3
  • 168
    • 0000525517 scopus 로고
    • A focusing Weissenberg camera with multi-layer-line screens for macromolecular crystallography
    • SAKABE, N. (1983). A focusing Weissenberg camera with multi-layer-line screens for macromolecular crystallography. J. Appl. Cryst. 16, 542-547.
    • (1983) J. Appl. Cryst. , vol.16 , pp. 542-547
    • Sakabe, N.1
  • 169
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation
    • SAKABE, N. (1991). X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instrum. & Methods A303, 448-463.
    • (1991) Nucl. Instrum. & Methods , vol.A303 , pp. 448-463
    • Sakabe, N.1
  • 170
    • 0001455061 scopus 로고
    • Weissenberg camera for macromolecules with imaging plate data collection system at the Photon Factory: Present status and future plan
    • SAKABE, N., IKEMIZU, S., SAKABE, K., HIGASHI, T., NAKAGAWA, A., WATANABE, N., ADACHI, S. & SASAKI, K. (1995). Weissenberg camera for macromolecules with imaging plate data collection system at the Photon Factory: Present status and future plan. Rev. Sci. Instrum. 66, 1276-1281.
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 1276-1281
    • Sakabe, N.1    Ikemizu, S.2    Sakabe, K.3    Higashi, T.4    Nakagawa, A.5    Watanabe, N.6    Adachi, S.7    Sasaki, K.8
  • 172
    • 0030214090 scopus 로고    scopus 로고
    • Buoyancy and surface-tension-driven convection in hanging drop protein crystallization
    • SAVINO, R. & MONTI, R. (1996). Buoyancy and surface-tension-driven convection in hanging drop protein crystallization. J. Cryst Growth 165, 308-318.
    • (1996) J. Cryst Growth , vol.165 , pp. 308-318
    • Savino, R.1    Monti, R.2
  • 173
    • 0028433688 scopus 로고
    • Effect of self-degradation products on crystallisation of protease thermolysin
    • SAZAKI, G., AOKI, S., OOSHIMA, H. & KATO, J. (1994). Effect of self-degradation products on crystallisation of protease thermolysin. J. Cryst Growth 139, 95-103.
    • (1994) J. Cryst Growth , vol.139 , pp. 95-103
    • Sazaki, G.1    Aoki, S.2    Ooshima, H.3    Kato, J.4
  • 174
    • 10544225419 scopus 로고    scopus 로고
    • Novel approach to measure the solubility of protein by using Michelson interferometry
    • in press
    • SAZAKI, G., YOSHIDA, E., NAKADA, T., MIYASHITA, S. & KOMATSU, H. (1996). Novel approach to measure the solubility of protein by using Michelson interferometry. J. Crystal Growth, in press.
    • (1996) J. Crystal Growth
    • Sazaki, G.1    Yoshida, E.2    Nakada, T.3    Miyashita, S.4    Komatsu, H.5
  • 175
    • 0002559125 scopus 로고
    • Crystallographic studies on p21 (H-Ras) using the synchrotron Laue method - Improvement of crystal quality and monitoring of the GTPase reaction at different time points
    • SCHEIDIG, A. J., SANCHEZ-LLORENTE, A., LAUTWEIN, A., PAI, E. F., CORRIE, J. E. T., REID, G. P., WITTINGHOFER, A. & GOODY, R. S. (1994). Crystallographic studies on p21 (H-Ras) using the synchrotron Laue method - Improvement of crystal quality and monitoring of the GTPase reaction at different time points. Acta Cryst. D 50, 512-520.
    • (1994) Acta Cryst. D , vol.50 , pp. 512-520
    • Scheidig, A.J.1    Sanchez-Llorente, A.2    Lautwein, A.3    Pai, E.F.4    Corrie, J.E.T.5    Reid, G.P.6    Wittinghofer, A.7    Goody, R.S.8
  • 176
    • 0000271093 scopus 로고
    • Feasibility of mapping solution properties during the growth of protein crystals
    • SCHLICHTA, P. J. (1986). Feasibility of mapping solution properties during the growth of protein crystals. J. Cryst. Growth 76, 656-662.
    • (1986) J. Cryst. Growth , vol.76 , pp. 656-662
    • Schlichta, P.J.1
  • 180
    • 0342932465 scopus 로고
    • Predispensed gradient matrices - A new rapid method of finding crystallisation conditions
    • SHAW STEWART, P. D. & KAHMISA, M. (1994). Predispensed gradient matrices - a new rapid method of finding crystallisation conditions. Acta Cryst. D 50, 441-442.
    • (1994) Acta Cryst. D , vol.50 , pp. 441-442
    • Shaw Stewart, P.D.1    Kahmisa, M.2
  • 181
    • 0002812783 scopus 로고
    • The application of direct methods and Patterson interpretation to high resolution native protein data
    • SHELDRICK, G., DAUTER, Z., WILSON, K. S., HOPE, H. AND SIEKER, L. (1994). The application of direct methods and Patterson interpretation to high resolution native protein data. Acta Cryst. D 49, 18-23.
    • (1994) Acta Cryst. D , vol.49 , pp. 18-23
    • Sheldrick, G.1    Dauter, Z.2    Wilson, K.S.3    Hope, H.4    Sieker, L.5
  • 182
    • 0000251982 scopus 로고
    • Elimination of twinning in crystals of Sulfolobus solfataricus alcohol dehydrogenase holo-enzyme by growth in agarose gels
    • SICA, F., DEMASI, D., MAZZARELLA, L., ZAGARI, A., CAPASSO, S., PEARL, L. H., D'AURIA, S., RAIA, C. A. & ROSSI, M. (1994). Elimination of twinning in crystals of Sulfolobus solfataricus alcohol dehydrogenase holo-enzyme by growth in agarose gels. Acta Cryst. D 50, 508-511.
    • (1994) Acta Cryst. D , vol.50 , pp. 508-511
    • Sica, F.1    Demasi, D.2    Mazzarella, L.3    Zagari, A.4    Capasso, S.5    Pearl, L.H.6    D'auria, S.7    Raia, C.A.8    Rossi, M.9
  • 183
    • 0027411179 scopus 로고
    • The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography
    • SINGER, P. T., SMALAS, A., CARTY, R. P., MANGEL, W. F. & SWEET, R. M. (1993). The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography. Science 259, 669-673.
    • (1993) Science , vol.259 , pp. 669-673
    • Singer, P.T.1    Smalas, A.2    Carty, R.P.3    Mangel, W.F.4    Sweet, R.M.5
  • 185
    • 0001718862 scopus 로고    scopus 로고
    • First ground trials of a Mach-Zehnder interferometer for implementation into a micrograyity protein crystallization facility - The APCF
    • SNELL, E. H., HELLIWELL, J. R., BOGGON, T. J., LAUTENSCHLAGER, P. & POTTHAST, L., (1996). First ground trials of a Mach-Zehnder interferometer for implementation into a micrograyity protein crystallization facility - the APCF. Acta Cryst. D 52, 529-533.
    • (1996) Acta Cryst. D , vol.52 , pp. 529-533
    • Snell, E.H.1    Helliwell, J.R.2    Boggon, T.J.3    Lautenschlager, P.4    Potthast, L.5
  • 186
    • 0026116759 scopus 로고
    • Protein crystallisation facilities for microgravity experiments
    • SNYDER, R. S., FUHRMANN, K. AND WALTER, H. U. (1991). Protein crystallisation facilities for microgravity experiments. J. Cryst. Growth 110, 333-338.
    • (1991) J. Cryst. Growth , vol.110 , pp. 333-338
    • Snyder, R.S.1    Fuhrmann, K.2    Walter, H.U.3
  • 187
    • 0027646150 scopus 로고
    • ASTEC: An automated system for sitting drop protein crystallisation
    • SORIANO, T. M. & FONTECILLA-CAMPS, J. C. (1993). ASTEC: an automated system for sitting drop protein crystallisation. J. Appl. Cryst. 26, 558-562.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 558-562
    • Soriano, T.M.1    Fontecilla-Camps, J.C.2
  • 188
    • 0029645585 scopus 로고
    • Direct measurement of reactivity in the protein crystal by steady-state kinetic-studies
    • STODDARD, B. L. & FARBER, G. K. (1995). Direct measurement of reactivity in the protein crystal by steady-state kinetic-studies. Structure 3, 991-996.
    • (1995) Structure , vol.3 , pp. 991-996
    • Stoddard, B.L.1    Farber, G.K.2
  • 189
    • 0012654747 scopus 로고    scopus 로고
    • An old technique with a new application: X-ray topography of protein crystals
    • STOJANOFF, V., SNELL, E. H., SIDDONS, D. P. & HELLIWELL, J. R. (1996). An old technique with a new application: X-ray topography of protein crystals. Synchrotron Radiation News 9, No. 1, 25-26.
    • (1996) Synchrotron Radiation News , vol.9 , Issue.1 , pp. 25-26
    • Stojanoff, V.1    Snell, E.H.2    Siddons, D.P.3    Helliwell, J.R.4
  • 190
    • 0026866113 scopus 로고
    • Long duration growth of protein crystals in microgravity aboard the MIR. space station
    • STRONG, R. K., STODDARD, B., ARROTT, A. & FARBER, G. K. (1992). Long duration growth of protein crystals in microgravity aboard the MIR. space station. J. Cryst. Growth 119, 200-214.
    • (1992) J. Cryst. Growth , vol.119 , pp. 200-214
    • Strong, R.K.1    Stoddard, B.2    Arrott, A.3    Farber, G.K.4
  • 194
    • 0027439826 scopus 로고
    • Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin
    • SUBRAMANIAM, S., GERSTEIN, M., OESTERHELT, D. & HENDERSON, R. (1993). Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO. J. 12, 1-8.
    • (1993) EMBO. J. , vol.12 , pp. 1-8
    • Subramaniam, S.1    Gerstein, M.2    Oesterhelt, D.3    Henderson, R.4
  • 195
    • 0002249964 scopus 로고
    • Fixed exit monochromators for high energy synchrotron radiation
    • SUORTTI, P. & SCHULZE, C. (1995). Fixed exit monochromators for high energy synchrotron radiation. J. Synchrotron Rad. 2, 6-12.
    • (1995) J. Synchrotron Rad. , vol.2 , pp. 6-12
    • Suortti, P.1    Schulze, C.2
  • 197
    • 0006081803 scopus 로고
    • The structure of the protein crambin from X-ray diffraction at 140 K
    • TEETER, M. M. & HOPE, H. (1986). The structure of the protein crambin from X-ray diffraction at 140 K. Ann NY Acad. Sci. 482, 163-165.
    • (1986) Ann NY Acad. Sci. , vol.482 , pp. 163-165
    • Teeter, M.M.1    Hope, H.2
  • 198
    • 0000434996 scopus 로고
    • Mounting of crystals for macromolecular crystallography in a free-standing thin film
    • TENG, T. Y. (1990). Mounting of crystals for macromolecular crystallography in a free-standing thin film. J. Appl. Cryst. 23, 387-391.
    • (1990) J. Appl. Cryst. , vol.23 , pp. 387-391
    • Teng, T.Y.1
  • 199
    • 0001656343 scopus 로고
    • The use of two novel methods to grow protein crystals by microdialysis and vapour diffusion in an agarose gel
    • THIESSEN, K. J. (1994). The use of two novel methods to grow protein crystals by microdialysis and vapour diffusion in an agarose gel. Acta Cryst. D 50, 491-495
    • (1994) Acta Cryst. D , vol.50 , pp. 491-495
    • Thiessen, K.J.1
  • 200
    • 0013577143 scopus 로고
    • A new macromolecular crystallography station (9.5) on the SRS Wiggler beam line for very rapid Laue and rapidly tunable monochromatic measurements: Commissioning and first results
    • THOMPSON, A. W., HABASH, J., HARROP, S. J., HELLIWELL, J. R., NAVE, C., ATKINSON, P., HASNAIN, S. S., GLOVER, I. D., MOORE, P. R., HARRIS, N., KINDER, S. & BUFFEY, S. (1992). A new macromolecular crystallography station (9.5) on the SRS Wiggler beam line for very rapid Laue and rapidly tunable monochromatic measurements: commissioning and first results. Rev. Sci. Instrum. 63(1), 1062-1064.
    • (1992) Rev. Sci. Instrum. , vol.63 , Issue.1 , pp. 1062-1064
    • Thompson, A.W.1    Habash, J.2    Harrop, S.J.3    Helliwell, J.R.4    Nave, C.5    Atkinson, P.6    Hasnain, S.S.7    Glover, I.D.8    Moore, P.R.9    Harris, N.10    Kinder, S.11    Buffey, S.12
  • 202
    • 0029132454 scopus 로고
    • Growth process of protein crystals revealed by laser Michelson interferometry investigation
    • VEKILOV, P. G., ATAKA, M. & KATSURA, T. (1995). Growth process of protein crystals revealed by laser Michelson interferometry investigation. Acta Cryst. D 51, 207-219.
    • (1995) Acta Cryst. D , vol.51 , pp. 207-219
    • Vekilov, P.G.1    Ataka, M.2    Katsura, T.3
  • 204
    • 0001141858 scopus 로고
    • On the disordered activation domain in trypsinogen: Chemical labelling and low temperature crystallography
    • WALTER, J., STEIGEMANN, W., SINGH, T. P., BARTUNIK, H., BODE, W. & HUBER, R. (1982). On the disordered activation domain in trypsinogen: chemical labelling and low temperature crystallography. Acta Cryst. B 38, 1462-1472.
    • (1982) Acta Cryst. B , vol.38 , pp. 1462-1472
    • Walter, J.1    Steigemann, W.2    Singh, T.P.3    Bartunik, H.4    Bode, W.5    Huber, R.6
  • 205
    • 0024035897 scopus 로고
    • Automatic preparation of protein crystals using laboratory robotics and automatic visual inspection
    • WARD, K. B., PEROZZO, M. A. & ZUK, W. M. (1988). Automatic preparation of protein crystals using laboratory robotics and automatic visual inspection. J. Cryst. Growth 90, 325-339.
    • (1988) J. Cryst. Growth , vol.90 , pp. 325-339
    • Ward, K.B.1    Perozzo, M.A.2    Zuk, W.M.3
  • 206
    • 0000722358 scopus 로고
    • Macromolecular crystallography at cryogenic temperatures
    • WATENPAUGH, K. D. (1991). Macromolecular crystallography at cryogenic temperatures. Curr. Opin. Struct. Biol. 1, 1012-1015.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 1012-1015
    • Watenpaugh, K.D.1
  • 207
    • 0009686487 scopus 로고
    • A protein crystallisation strategy using automated grid searches on successively finer grids
    • WEBER, P. C. (1990). A protein crystallisation strategy using automated grid searches on successively finer grids. Methods: a companion to Methods in Enzymology. 1, 31-37.
    • (1990) Methods: A Companion to Methods in Enzymology , vol.1 , pp. 31-37
    • Weber, P.C.1
  • 208
    • 0000506911 scopus 로고
    • High resolution crystallographic studies of native concanavalin A using rapid Laue data collection methods and the introduction of a monochromatic large-angle oscillation technique (LOT)
    • WEISGERBER, S. & HELLIWELL, J. R. (1993). High resolution crystallographic studies of native concanavalin A using rapid Laue data collection methods and the introduction of a monochromatic large-angle oscillation technique (LOT). Faraday Transactions, 89(15), 2667-2675.
    • (1993) Faraday Transactions , vol.89 , Issue.15 , pp. 2667-2675
    • Weisgerber, S.1    Helliwell, J.R.2
  • 210
    • 0000638115 scopus 로고
    • Quasi-Laue neutron diffractometer
    • WILKINSON, C. & LEHMANN, M. (1991). Quasi-Laue neutron diffractometer. Nucl. Instrum. & Methods 310(1-2), 411-415.
    • (1991) Nucl. Instrum. & Methods , vol.310 , Issue.1-2 , pp. 411-415
    • Wilkinson, C.1    Lehmann, M.2
  • 211
    • 0026335459 scopus 로고
    • Crystallisation and preliminary X-ray data for the negative regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa
    • WILSON, S. A., CHAYEN, N., HEMMINGS, A. M., DREW, R. E. & PEARL, L. H. (1991). Crystallisation and preliminary X-ray data for the negative regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa. J. Mol. Biol. 222, 869-871.
    • (1991) J. Mol. Biol. , vol.222 , pp. 869-871
    • Wilson, S.A.1    Chayen, N.2    Hemmings, A.M.3    Drew, R.E.4    Pearl, L.H.5
  • 213
    • 0020449148 scopus 로고
    • Parameters for crystal growth of ribosomal subunits
    • YONATH, A., MUSSING, J. & WITTMAN, H. G. (1982). Parameters for crystal growth of ribosomal subunits. J. Cell Biochem. 19, 145-155.
    • (1982) J. Cell Biochem. , vol.19 , pp. 145-155
    • Yonath, A.1    Mussing, J.2    Wittman, H.G.3
  • 214
    • 0027610433 scopus 로고
    • Comparison of radiation-induced decay and structure refinement from X-ray data collected from lysozyme crystals at low and ambient temperatures
    • YOUNG, A. C. M., DEWAN, J. C., NAVE, C. & TILTON, R. F. (1993). Comparison of radiation-induced decay and structure refinement from X-ray data collected from lysozyme crystals at low and ambient temperatures. J. Appl. Cryst. 26, 309-319.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 309-319
    • Young, A.C.M.1    Dewan, J.C.2    Nave, C.3    Tilton, R.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.