메뉴 건너뛰기




Volumn 4, Issue 11, 1997, Pages 909-914

Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ENZYME STRUCTURE; IMAGING SYSTEM; NEUTRON; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

EID: 0030694240     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1197-909     Document Type: Review
Times cited : (151)

References (39)
  • 1
    • 0343003638 scopus 로고
    • Protein structure determination by neutron diffraction: Lysozyme
    • Bentley, G.A., Duee, E.D., Mason, S.A. & Nunes, A.C. Protein structure determination by neutron diffraction: lysozyme. J. Chim. Phys. 76, 817-821 (1979).
    • (1979) J. Chim. Phys. , vol.76 , pp. 817-821
    • Bentley, G.A.1    Duee, E.D.2    Mason, S.A.3    Nunes, A.C.4
  • 2
    • 0019827532 scopus 로고
    • Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin
    • Phillips, S.E.V. & Schoenborn, B.P. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature 292, 81-82 (1981).
    • (1981) Nature , vol.292 , pp. 81-82
    • Phillips, S.E.V.1    Schoenborn, B.P.2
  • 3
    • 14444272390 scopus 로고
    • Hydration in protein crystals. A neutron diffraction analysis of carbonmonoxymyoglobin
    • Cheng, X. & Schoenborn, B.P. Hydration in protein crystals. A neutron diffraction analysis of carbonmonoxymyoglobin. Acta Crystallogr. B46, 195-208 (1990).
    • (1990) Acta Crystallogr. , vol.B46 , pp. 195-208
    • Cheng, X.1    Schoenborn, B.P.2
  • 4
    • 0024292806 scopus 로고
    • Solvent effect in protein crystals - A neutron diffraction analysis of solvent and ion density
    • Schoenborn, B.P. Solvent effect in protein crystals - A neutron diffraction analysis of solvent and ion density. J. Mol. Biol. 201, 741-749 (1988).
    • (1988) J. Mol. Biol. , vol.201 , pp. 741-749
    • Schoenborn, B.P.1
  • 5
    • 0019889789 scopus 로고
    • Direct determination of protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin
    • Kossiakoff, A.A. & Spencer, S.A. Direct determination of protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin. Biochemistry 20, 6462-6474 (1981).
    • (1981) Biochemistry , vol.20 , pp. 6462-6474
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 6
    • 0019334147 scopus 로고
    • Neutron diffraction identifies his-57 as the catalytic base in trypsin
    • Kossiakoff, A.A. & Spencer, S.A. Neutron diffraction identifies his-57 as the catalytic base in trypsin. Nature 288, 414-416 (1980).
    • (1980) Nature , vol.288 , pp. 414-416
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 7
    • 0026547998 scopus 로고
    • Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction
    • Finer-Moore, J.S., Kossiakoff, A.A., Hurley, J.H., Earnest, T. & Stroud, R.M. Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction. Proteins 12, 203-222 (1992).
    • (1992) Proteins , vol.12 , pp. 203-222
    • Finer-Moore, J.S.1    Kossiakoff, A.A.2    Hurley, J.H.3    Earnest, T.4    Stroud, R.M.5
  • 9
    • 0020772531 scopus 로고
    • Active site of RNase: Neutron diffraction study of a complex with uridine vanadate, a transition-state analog
    • Wlodawer, A., Miller, M. & Sjolin, L. Active site of RNase: neutron diffraction study of a complex with uridine vanadate, a transition-state analog. Proc. Natl. Acad. Sci. USA 80, 3628-3631 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3628-3631
    • Wlodawer, A.1    Miller, M.2    Sjolin, L.3
  • 10
    • 0004259377 scopus 로고
    • Hydrogen exchange in RNase A: Neutron diffraction study
    • Wlodawer, A. & Sjolin, L. Hydrogen exchange in RNase A: Neutron diffraction study, Proc. Natl. Acad. Sci. USA 79, 1418-1422 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1418-1422
    • Wlodawer, A.1    Sjolin, L.2
  • 11
    • 84944814721 scopus 로고
    • Comparison of two independently refined models of RNase A
    • Wlodawer, A., Borkakoti, N., Moss, D.S. & Howlin, B. Comparison of two independently refined models of RNase A. Acta Crystallogr. B42, 379-387 (1986).
    • (1986) Acta Crystallogr. , vol.B42 , pp. 379-387
    • Wlodawer, A.1    Borkakoti, N.2    Moss, D.S.3    Howlin, B.4
  • 12
    • 0021603710 scopus 로고
    • Structure of bovine pancreatic trypsin inhibitor - Results of joint neutron and X-ray refinement of crystal form IL
    • Wlodawer, A., Walter, J., Huber, R. & Sjolin, L. Structure of bovine pancreatic trypsin inhibitor - results of joint neutron and X-ray refinement of crystal form IL J. Mol. Biol. 180, 301-329 (1984).
    • (1984) J. Mol. Biol. , vol.180 , pp. 301-329
    • Wlodawer, A.1    Walter, J.2    Huber, R.3    Sjolin, L.4
  • 13
    • 0023120307 scopus 로고
    • Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor
    • Wlodawer, A., Deisenhofer, J. & Huber, R. Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor J. Mol. Biol. 193, 145-156 (1987).
    • (1987) J. Mol. Biol. , vol.193 , pp. 145-156
    • Wlodawer, A.1    Deisenhofer, J.2    Huber, R.3
  • 14
    • 0026977749 scopus 로고
    • Multilayer monochromators and supermirrors for neutron protein crystallography using a quasi Laue technique
    • Schoenborn, B.P. Multilayer monochromators and supermirrors for neutron protein crystallography using a quasi Laue technique, SPIE (Society of Photooptical instrumentation engineers) 1738, 192-198 (1992).
    • (1992) SPIE (Society of Photo-optical Instrumentation Engineers) , vol.1738 , pp. 192-198
    • Schoenborn, B.P.1
  • 15
    • 0000638115 scopus 로고
    • Quasi-Laue neutron diffractometer Nucl
    • Wilkinson, C. & Lehmann, M.S. quasi-Laue neutron diffractometer Nucl. Instrm. Meths A310, 411-415 (1991).
    • (1991) Instrm. Meths , vol.A310 , pp. 411-415
    • Wilkinson, C.1    Lehmann, M.S.2
  • 18
    • 0028517055 scopus 로고
    • An imaging plate neutron detector
    • Niimura, N. et al. An imaging plate neutron detector. Nucl. Instrm. Meths A349, 521-525 (1994).
    • (1994) Nucl. Instrm. Meths , vol.A349 , pp. 521-525
    • Niimura, N.1
  • 19
  • 20
    • 33645072545 scopus 로고
    • A large single crystal of the tetragonal form of lysozyme can be grown in a concentration gradient of NiCI2
    • Ataka, M. & Katsura, T. A large single crystal of the tetragonal form of lysozyme can be grown in a concentration gradient of NiCI2. JAERI-M (Japan Atomic Energy Research Institute-Memos) 61, 92-213 (1992).
    • (1992) JAERI-M (Japan Atomic Energy Research Institute-Memos) , vol.61 , pp. 92-213
    • Ataka, M.1    Katsura, T.2
  • 21
    • 0021291297 scopus 로고
    • Deuterium exchange in lysozyme at 1.4 Å resolution
    • (ed Schoenborn, B.P.) (Plenum Press, New York and London)
    • Mason, S.A., Bentley, G.A., & McIntyre, G.J. Deuterium exchange in lysozyme at 1.4 Å resolution. Neutron in Biology. (ed Schoenborn, B.P.) 323-334 (Plenum Press, New York and London;1984).
    • (1984) Neutron in Biology , pp. 323-334
    • Mason, S.A.1    Bentley, G.A.2    McIntyre, G.J.3
  • 22
    • 0001475908 scopus 로고
    • The recording and analysis of synchrotron X-radiation Laue diffraction photographs
    • Helliwell, J.R. et al. The recording and analysis of synchrotron X-radiation Laue diffraction photographs. J. Appl. Crystallogr. 22, 483-497 (1989).
    • (1989) J. Appl. Crystallogr. , vol.22 , pp. 483-497
    • Helliwell, J.R.1
  • 23
    • 0000578877 scopus 로고
    • Angular distribution of reflections in Laue diffraction
    • Cruickshank, D.W.J., Helliwell, J.R. & Moffat, K. Angular distribution of reflections in Laue diffraction. Acta Crystallogr. A47, 352-373 (1991).
    • (1991) Acta Crystallogr , vol.A47 , pp. 352-373
    • Cruickshank, D.W.J.1    Helliwell, J.R.2    Moffat, K.3
  • 24
    • 0026202158 scopus 로고
    • Experimental strategies in Laue crystallography
    • Clifton, I.J., Elder, M. & Hajdu, J. Experimental strategies in Laue crystallography. J. Appl. Crystallogr. 24, 267-277 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 267-277
    • Clifton, I.J.1    Elder, M.2    Hajdu, J.3
  • 25
    • 0026853347 scopus 로고
    • Estimation of dmin, min and max from the gnomonic projections of Laue patterns
    • Cruickshank, D.W.J., Carr, P.D. & Harding, M.M. Estimation of dmin, min and max from the gnomonic projections of Laue patterns. J. Appl. Crystallogr. 25, 285-293 (1992).
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 285-293
    • Cruickshank, D.W.J.1    Carr, P.D.2    Harding, M.M.3
  • 26
    • 0001603911 scopus 로고
    • Structure determination of turkey egg-white lysozyme using Laue diffraction data
    • Howell, P.L., Almo, S.C., Parsons, M.R., Harjdu, J. & Petsko, G.A. Structure determination of turkey egg-white lysozyme using Laue diffraction data. Acta Crystallogr. B48, 200-207 (1992).
    • (1992) Acta Crystallogr. , vol.B48 , pp. 200-207
    • Howell, P.L.1    Almo, S.C.2    Parsons, M.R.3    Harjdu, J.4    Petsko, G.A.5
  • 27
    • 0013544951 scopus 로고
    • Determination of dmin and min from the intensity distributions of Laue patterns
    • Hao, Q., Harding, M.M. & Campbell, J.W. Determination of dmin and min from the intensity distributions of Laue patterns. J. Appl. Crystallogr. 28, 447-450 (1995).
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 447-450
    • Hao, Q.1    Harding, M.M.2    Campbell, J.W.3
  • 28
    • 0542375063 scopus 로고
    • Spatial-distortion corrections, for Laue diffraction patterns recorded on image plates, modelled using polynomial functions
    • Campbell, J.W., Harding, M.M. & Kariuki, B. Spatial-distortion corrections, for Laue diffraction patterns recorded on image plates, modelled using polynomial functions. J. Appl. Crystallogr. 26, 43-48 (1995).
    • (1995) J. Appl. Crystallogr. , vol.26 , pp. 43-48
    • Campbell, J.W.1    Harding, M.M.2    Kariuki, B.3
  • 29
    • 0008031063 scopus 로고
    • The Laue data module (LDM) - A software development for Laue X-ray diffraction data processing
    • Campbell, J.W., Clifton, I.J., Harding, M.M. & Hao, Q. The Laue data module (LDM) - a software development for Laue X-ray diffraction data processing. J. Appl. Crystallogr. 28, 635-640 (1995).
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 635-640
    • Campbell, J.W.1    Clifton, I.J.2    Harding, M.M.3    Hao, Q.4
  • 30
    • 0001405524 scopus 로고
    • LAUEGEN, an X-windows-based program for the processing of Laue X-ray diffraction data
    • Campbell, J.W. LAUEGEN, an X-windows-based program for the processing of Laue X-ray diffraction data. J. Appl. Crystallogr. 28, 228-236 (1995).
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 228-236
    • Campbell, J.W.1
  • 31
    • 0000695363 scopus 로고    scopus 로고
    • High resolution structure (1.33 Å) of HEW lysozyme tetragonal crystal grown in the APCF Apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission
    • Vaney, M.C., Maignan, S., Ries-Kautt, M., & Ducruix, A., High resolution structure (1.33 Å) of HEW lysozyme tetragonal crystal grown in the APCF Apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Acta Crystallogr. D52, 505-517 (1996).
    • (1996) Acta Crystallogr. , vol.D52 , pp. 505-517
    • Vaney, M.C.1    Maignan, S.2    Ries-Kautt, M.3    Ducruix, A.4
  • 32
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. & Karplus, M., Crystallographic R factor refinement by molecular dynamics, Science 235, 458-460 (1987).
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 33
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing -Application to a 2.8 Å resolution structure of aspartate aminotransferase
    • Brünger, A.T. Crystallographic refinement by simulated annealing -Application to a 2.8 Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203, 803-816 (1988).
    • (1988) J. Mol. Biol. , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 34
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger, A.T., Crystallographic refinement by simulated annealing: Application to crambin. Acta Crystallogr. A45, 50-61 (1989).
    • (1989) Acta Crystallogr. , vol.A45 , pp. 50-61
    • Brünger, A.T.1
  • 36
    • 0013971370 scopus 로고
    • The three-dimensional structure of an enzyme molecule
    • Phillips, D.C. The three-dimensional structure of an enzyme molecule. Sci. Am. 215 (5), 78-90 (1966).
    • (1966) Sci. Am. , vol.215 , Issue.5 , pp. 78-90
    • Phillips, D.C.1
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 39
    • 0028057108 scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • Merritt, Ethan A. & Murphy, Michael E.P. Raster3D version 2.0: a program for photorealistic molecular graphics Acta Crystallogr. D50, 869-873 (1994).
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.