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1
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0029777433
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Intermediate trapping and Laue X-ray diffraction: Potential for enzyme mechanism, dynamics, and inhibitor screening
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Stoddard BL. Intermediate trapping and Laue X-ray diffraction: potential for enzyme mechanism, dynamics, and inhibitor screening. Pharmacol Ther. 70:1996;215-256.
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Stoddard, B.L.1
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0029861873
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Caught in a chemical trap
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Stoddard BL. Caught in a chemical trap. Nat Struct Biol. 3:1996;907-909.
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Nat Struct Biol
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Stoddard, B.L.1
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0030766991
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Laue diffraction
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of outstanding interest. C. Carter, Sweet R.M. Academic Press, San Diego, The newest installment of 'Diffraction Methods' in the Methods in Enzymology series includes the most up-to-date and detailed description of the Laue diffraction method for macromolecules, including copious detail on experimental protocols
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Moffat K. Laue diffraction. of outstanding interest Carter C, Sweet RM. Methods in Enzymology. 1997;433-447 Academic Press, San Diego, The newest installment of 'Diffraction Methods' in the Methods in Enzymology series includes the most up-to-date and detailed description of the Laue diffraction method for macromolecules, including copious detail on experimental protocols.
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(1997)
Methods in Enzymology
, pp. 433-447
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Moffat, K.1
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4
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0030833143
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Synchrotron radiation applications to macromolecular crystallography
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Moffat K, Ren Z. Synchrotron radiation applications to macromolecular crystallography. Curr Opin Struct Biol. 7:1997;689-696.
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Curr Opin Struct Biol
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Moffat, K.1
Ren, Z.2
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5
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0028874533
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Freeze trapping of reaction intermediates
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Moffat K, Henderson R. Freeze trapping of reaction intermediates. Curr Opin Struct Biol. 5:1995;656-663.
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Curr Opin Struct Biol
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Moffat, K.1
Henderson, R.2
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6
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0028774714
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Cryocrystallography
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Rodgers DW. Cryocrystallography. Structure. 2:1994;1135-1140.
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Structure
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Rodgers, D.W.1
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7
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0026720247
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Crystalline ribonuclease A loses function below the dynamic transition at 220K
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Rasmussen BF, Stock A, Ringe D, Petsko GA. Crystalline ribonuclease A loses function below the dynamic transition at 220K. Nature. 357:1992;423-426.
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Nature
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, pp. 423-426
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Rasmussen, B.F.1
Stock, A.2
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8
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0028243728
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X-ray crystal structure of γ-chymotrypsin in hexane
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Yennewar NH, Yennewar HP, Farber GK. X-ray crystal structure of γ-chymotrypsin in hexane. Biochemistry. 33:1994;7326-7336.
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Biochemistry
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Yennewar, N.H.1
Yennewar, H.P.2
Farber, G.K.3
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9
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0029024462
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Mutagenesis and Laue structures of enzyme intermediates: Isocitrate dehydrogenase
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Bolduc JM, Dyer DM, Scott WG, Singer P, Sweet RM, Koshland DE, Stoddard BL. Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Science. 268:1995;1312-1318.
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Science
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Bolduc, J.M.1
Dyer, D.M.2
Scott, W.G.3
Singer, P.4
Sweet, R.M.5
Koshland, D.E.6
Stoddard, B.L.7
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10
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33751195297
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Neutron laue diffraction study of concanavalin A
-
of outstanding interest. One of two studies [11] reported in the past year on macromolecular neutron diffraction studies using a polychromatic source and subsequent data reduction. This study was shown to be in good agreement with previous monochromatic neutron diffraction studies of the same protein. It is proposed that this new method will help to open up the technique to larger proteins and/or smaller crystals.
-
Habash J, Raftery J, Wisgerber S, Cassetta A, Lehmann MS, Hoghoj P, Wilkinson C, Campbell JW, Helliwell JR. Neutron laue diffraction study of concanavalin A. of outstanding interest Faraday Trans. 93:1997;4313-4317 One of two studies [11] reported in the past year on macromolecular neutron diffraction studies using a polychromatic source and subsequent data reduction. This study was shown to be in good agreement with previous monochromatic neutron diffraction studies of the same protein. It is proposed that this new method will help to open up the technique to larger proteins and/or smaller crystals.
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(1997)
Faraday Trans
, vol.93
, pp. 4313-4317
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Habash, J.1
Raftery, J.2
Wisgerber, S.3
Cassetta, A.4
Lehmann, M.S.5
Hoghoj, P.6
Wilkinson, C.7
Campbell, J.W.8
Helliwell, J.R.9
-
11
-
-
0030694240
-
Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography
-
of outstanding interest. A second study [10], reported to 2 Å resolution by an independent group, on neutron diffraction of a macromolecular crystal (lysozyme) using the Laue method. An adaptation of existing detector geometry and processing software is described for the reduction of the data.
-
Niimura N, Minezaki Y, Nonaka T, Castagna J-C, Cipriani F, Hoghoj P, Lehmann MS, Wilkinson C. Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography. of outstanding interest Nat Struct Biol. 4:1997;909-914 A second study [10], reported to 2 Å resolution by an independent group, on neutron diffraction of a macromolecular crystal (lysozyme) using the Laue method. An adaptation of existing detector geometry and processing software is described for the reduction of the data.
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(1997)
Nat Struct Biol
, vol.4
, pp. 909-914
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Niimura, N.1
Minezaki, Y.2
Nonaka, T.3
Castagna J-C4
Cipriani, F.5
Hoghoj, P.6
Lehmann, M.S.7
Wilkinson, C.8
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12
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0030715546
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Neutron Laue diffraction does it faster
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Helliwell JR. Neutron Laue diffraction does it faster. Nat Struct Biol. 4:1998;874-876.
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Nat Struct Biol
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, pp. 874-876
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Helliwell, J.R.1
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13
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0028898295
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Optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals
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Ng K, Getzoff ED, Moffat K. Optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals. Biochemistry. 34:1995;879-889.
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Biochemistry
, vol.34
, pp. 879-889
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Ng, K.1
Getzoff, E.D.2
Moffat, K.3
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14
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0024730905
-
Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery
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Meyer TE, Tollin G, Hazzard JH, Cusanovich MA. Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery. Biophys J. 56:1989;559-564.
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Meyer, T.E.1
Tollin, G.2
Hazzard, J.H.3
Cusanovich, M.A.4
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15
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0029803844
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Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy
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Imamoto Y, Kataoka M, Tokunaga F. Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy. Biochemistry. 35:1996;14047-14053.
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Biochemistry
, vol.35
, pp. 14047-14053
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Imamoto, Y.1
Kataoka, M.2
Tokunaga, F.3
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16
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0028100905
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Measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila
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Hoff WD, Hellingwerff KJ. Measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila. Biophys J. 67:1994;1691-1705.
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Hoff, W.D.1
Hellingwerff, K.J.2
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0029110488
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1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
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Borgstahl GEO, Williams DR, Getzoff ED. 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry. 34:1995;6278-6287.
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Biochemistry
, vol.34
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Borgstahl, G.E.O.1
Williams, D.R.2
Getzoff, E.D.3
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18
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0031039399
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Structure of a protein photocycle intermediate by millisecond time-resolved crystallography
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Genick UK, Borgstahl GEO, Ng K, Ren Z, Pradervand C, Burke PM, Srajer V, Teng T-Y, Schildkamp W, McRee DE, et al. Structure of a protein photocycle intermediate by millisecond time-resolved crystallography. Science. 275:1997;1471-1475.
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Science
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, pp. 1471-1475
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Genick, U.K.1
Borgstahl, G.E.O.2
Ng, K.3
Ren, Z.4
Pradervand, C.5
Burke, P.M.6
Srajer, V.7
Teng T-Y8
Schildkamp, W.9
McRee, D.E.10
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19
-
-
0032510475
-
Structure at 0.85 Å resolution of an early protein photocycle intermediate
-
* intermediate of the PYP photocycle was trapped by photoisomerization at -100°C and its structure determined at 0.85 Å resolution. The structure demonstrated isomerization through a flip of the thioester linkage between the chromophore and protein and the isomerized bond is shown to be trapped in a conformation resembling that of the transition state
-
* intermediate of the PYP photocycle was trapped by photoisomerization at -100°C and its structure determined at 0.85 Å resolution. The structure demonstrated isomerization through a flip of the thioester linkage between the chromophore and protein and the isomerized bond is shown to be trapped in a conformation resembling that of the transition state.
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(1998)
Nature
, vol.392
, pp. 206-209
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Genick, U.K.1
Soltis, S.M.2
Kuhn, P.3
Canestrelli, I.L.4
Getzoff, E.D.5
-
20
-
-
7144253808
-
Energy transduction on the nanosecond time scale: Early structural events in a xanthopsin photocycle
-
L) intermediate using rapid excitation followed by 150 ps Laue X-ray exposures taken 1 ns after the excitation event. The resulting structure demonstrates the same flip of the thioester linkage and shows the chromophore geometry after complete isomerization to a fully trans-conformation. The main conformational motions of the surrounding protein are consistent with the cryotrapped structure [19].
-
L) intermediate using rapid excitation followed by 150 ps Laue X-ray exposures taken 1 ns after the excitation event. The resulting structure demonstrates the same flip of the thioester linkage and shows the chromophore geometry after complete isomerization to a fully trans-conformation. The main conformational motions of the surrounding protein are consistent with the cryotrapped structure [19].
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(1998)
Science
, vol.279
, pp. 1946-1950
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-
Perman, B.1
Srajer, V.2
Ren, Z.3
Teng T-Y4
Pradervand, C.5
Ursby, T.6
Bourgeois, D.7
Schotte, F.8
Wulff, M.9
Kort, R.10
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21
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0031172844
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Laue crystallography: Lights! camera! action!
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Farber GK. Laue crystallography: lights! camera! action! Curr Biol. 7:1997;R352-R354.
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(1997)
Curr Biol
, vol.7
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Farber, G.K.1
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22
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0031570664
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Out of the blue: The photocycle of the photoactive yellow protein
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Schlichting I, Berendzen J. Out of the blue: the photocycle of the photoactive yellow protein. Structure. 5:1997;735-739.
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(1997)
Structure
, vol.5
, pp. 735-739
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Schlichting, I.1
Berendzen, J.2
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24
-
-
0028519126
-
Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
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Teng T-Y, Srajer V, Moffat K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nat Struct Biol. 1:1994;701-705.
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(1994)
Nat Struct Biol
, vol.1
, pp. 701-705
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Teng T-Y1
Srajer, V.2
Moffat, K.3
-
25
-
-
10544231457
-
Photolysis of the carbon monoxide complex of myoglobin: Nanosecond time-resolved crystallography
-
Srajer V, Teng T-Y, Ursby T, Pradervand C, Ren Z, Adachi S-I, Schildkamp W, Bourgeois D, Wulff M, Moffat K. Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography. Science. 274:1996;1726-1729.
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(1996)
Science
, vol.274
, pp. 1726-1729
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Srajer, V.1
Teng T-Y2
Ursby, T.3
Pradervand, C.4
Ren, Z.5
Adachi S-I6
Schildkamp, W.7
Bourgeois, D.8
Wulff, M.9
Moffat, K.10
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26
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0029849618
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Nanosecond crystallographic snapshots of protein structural changes
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Eaton WA, Henry ER, Hofrichter J. Nanosecond crystallographic snapshots of protein structural changes. Science. 274:1996;1631-1632.
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(1996)
Science
, vol.274
, pp. 1631-1632
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Eaton, W.A.1
Henry, E.R.2
Hofrichter, J.3
-
27
-
-
0030821996
-
Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures
-
of outstanding interest. A series of low temperature Laue structures of carbon monoxide - myoglobin after photolysis is reported. They help map the trajectory and dynamics of ligand migration in the binding cavity after dissociation. The results of this study account for the different locations of the carbon monoxide molecule that were previously reported in three cryocrystallographic trapping studies and are in agreement with theoretical predictions of carbon monoxide probability distributions.
-
Teng TY, Srajer V, Moffat K. Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures. of outstanding interest Biochemistry. 36:1997;12087-12100 A series of low temperature Laue structures of carbon monoxide - myoglobin after photolysis is reported. They help map the trajectory and dynamics of ligand migration in the binding cavity after dissociation. The results of this study account for the different locations of the carbon monoxide molecule that were previously reported in three cryocrystallographic trapping studies and are in agreement with theoretical predictions of carbon monoxide probability distributions.
-
(1997)
Biochemistry
, vol.36
, pp. 12087-12100
-
-
Teng, T.Y.1
Srajer, V.2
Moffat, K.3
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28
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0028063567
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Three-dimensional structure of a hammerhead ribozyme
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Pley HW, Flaherty KM, McKay DB. Three-dimensional structure of a hammerhead ribozyme. Nature. 372:1994;68-74.
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(1994)
Nature
, vol.372
, pp. 68-74
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Pley, H.W.1
Flaherty, K.M.2
McKay, D.B.3
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29
-
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0029073091
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The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
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Scott WG, Finch JT, Klug A. The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage. Cell. 81:1995;991-1002.
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(1995)
Cell
, vol.81
, pp. 991-1002
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Scott, W.G.1
Finch, J.T.2
Klug, A.3
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30
-
-
0030476765
-
Capturing the structure of a catalytic RNA intermediate: The hammerhead ribozyme
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Scott WG, Murray JB, Arnold JRP, Stoddard BL, Klug A. Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme. Science. 274:1996;2065-2069.
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(1996)
Science
, vol.274
, pp. 2065-2069
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Scott, W.G.1
Murray, J.B.2
Arnold, J.R.P.3
Stoddard, B.L.4
Klug, A.5
-
31
-
-
0032489357
-
The structural basis of hammerhead ribozyme self-cleavage
-
of outstanding interest. An 8.7 Å conformational change that takes place in the cleavage site of the hammerhead ribozyme was captured using chemical trapping (by perturbation of the substrate through the incorporation of a 5'-C-methyl group on the leaving group), followed by pH triggering and cryogenic trapping. The rearrangement brings the hammerhead ribozyme from the ground state into a conformation that resembles the transition-state geometry required for hammerhead RNA self-cleavage.
-
Murray JB, Terwey DP, Maloney L, Karpeisky A, Usman N, Beigelman L, Scott WG. The structural basis of hammerhead ribozyme self-cleavage. of outstanding interest Cell. 92:1998;665-673 An 8.7 Å conformational change that takes place in the cleavage site of the hammerhead ribozyme was captured using chemical trapping (by perturbation of the substrate through the incorporation of a 5'-C-methyl group on the leaving group), followed by pH triggering and cryogenic trapping. The rearrangement brings the hammerhead ribozyme from the ground state into a conformation that resembles the transition-state geometry required for hammerhead RNA self-cleavage.
-
(1998)
Cell
, vol.92
, pp. 665-673
-
-
Murray, J.B.1
Terwey, D.P.2
Maloney, L.3
Karpeisky, A.4
Usman, N.5
Beigelman, L.6
Scott, W.G.7
-
32
-
-
0032474760
-
DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-Ppol
-
of special interest. The structure of a novel site-specific homing endonuclease was determined at 1.8 Å resolution. As part of the initial structural description, the enzyme was visualized as both a cleaved product complex (with a bound divalent magnesium ion) and trapped as an uncleaved substrate complex (by the incorporation of a thiol sulfur at the 3'-hydroxyl leaving group position). A significant conformational change of both several sidechains and the labile phosphate occurs as a result of bond cleavage.
-
Flick KE, Jurica MS, Monnat RJ, Stoddard BL. DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-Ppol. of special interest Nature. 394:1998;96-101 The structure of a novel site-specific homing endonuclease was determined at 1.8 Å resolution. As part of the initial structural description, the enzyme was visualized as both a cleaved product complex (with a bound divalent magnesium ion) and trapped as an uncleaved substrate complex (by the incorporation of a thiol sulfur at the 3'-hydroxyl leaving group position). A significant conformational change of both several sidechains and the labile phosphate occurs as a result of bond cleavage.
-
(1998)
Nature
, vol.394
, pp. 96-101
-
-
Flick, K.E.1
Jurica, M.S.2
Monnat, R.J.3
Stoddard, B.L.4
-
33
-
-
0030768043
-
Trapping and visualization of a covalent enzyme-phosphate intermediate
-
of outstanding interest. Using a point mutant of alkaline phosphatase, a covalent phosphoenzyme intermediate was trapped by room temperature steady-state accumulation and visualized at 2.3 Å resolution. The structure reveals a catalytic water molecule bound to one of the active site zinc ions; it is ideally positioned for the apical attack that is necessary for the hydrolysis of the intermediate.
-
Murphy J, Stec B, Ma L, Kantrowitz ER. Trapping and visualization of a covalent enzyme-phosphate intermediate. of outstanding interest Nat Struct Biol. 4:1997;618-621 Using a point mutant of alkaline phosphatase, a covalent phosphoenzyme intermediate was trapped by room temperature steady-state accumulation and visualized at 2.3 Å resolution. The structure reveals a catalytic water molecule bound to one of the active site zinc ions; it is ideally positioned for the apical attack that is necessary for the hydrolysis of the intermediate.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 618-621
-
-
Murphy, J.1
Stec, B.2
Ma, L.3
Kantrowitz, E.R.4
-
34
-
-
0030765355
-
Crystal structure of a trapped phosphoenzyme during a catalytic reaction
-
of outstanding interest. A study that is similar in nature to the work described in [33] involved trapping a phosphohistidine intermediate of the reaction catalyzed by fructose-2,6-bisphosphatase. Rapid cryotrapping was used to capture the intermediate. The geometry of the complex suggests that the dephosphorylation step requires the prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water molecule.
-
Lee Y-H, Olson TW, Ogata CM, Levitt DG, Banaszak LJ, Lange AJ. Crystal structure of a trapped phosphoenzyme during a catalytic reaction. of outstanding interest Nat Struct Biol. 4:1997;615-618 A study that is similar in nature to the work described in [33] involved trapping a phosphohistidine intermediate of the reaction catalyzed by fructose-2,6-bisphosphatase. Rapid cryotrapping was used to capture the intermediate. The geometry of the complex suggests that the dephosphorylation step requires the prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water molecule.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 615-618
-
-
Lee Y-H1
Olson, T.W.2
Ogata, C.M.3
Levitt, D.G.4
Banaszak, L.J.5
Lange, A.J.6
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35
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0024392725
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Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase
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Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE, Stroud RM. Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc Natl Acad Sci USA. 86:1989;8635-8639.
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(1989)
Proc Natl Acad Sci USA
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, pp. 8635-8639
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Hurley, J.H.1
Thorsness, P.E.2
Ramalingam, V.3
Helmers, N.H.4
Koshland, D.E.5
Stroud, R.M.6
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36
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0025032116
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Regulation of an enzyme by phosphorylation at the active site
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Hurley JH, Dean AM, Sohl JL, Koshland DE, Stroud RM. Regulation of an enzyme by phosphorylation at the active site. Science. 249:1990;1012-1016.
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(1990)
Science
, vol.249
, pp. 1012-1016
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Hurley, J.H.1
Dean, A.M.2
Sohl, J.L.3
Koshland, D.E.4
Stroud, R.M.5
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37
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0025217677
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Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme
-
Hurley JH, Dean AM, Thorsness PE, Koshland DE, Stroud RM. Regulation of isocitrate dehydrogenase by phosphorylation involves no long-range conformational change in the free enzyme. J Biol Chem. 265:1990;3599-3602.
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(1990)
J Biol Chem
, vol.265
, pp. 3599-3602
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Hurley, J.H.1
Dean, A.M.2
Thorsness, P.E.3
Koshland, D.E.4
Stroud, R.M.5
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38
-
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0026094361
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Catalytic mechanism of NADP-dependent isocitrate dehydrogenase: Implications from the structures of magnesium-isocitrate and NADP complexes
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Hurley JH, Dean AM, Koshland DE, Stroud RM. Catalytic mechanism of NADP-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP complexes. Biochemistry. 30:1991;8671-8678.
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(1991)
Biochemistry
, vol.30
, pp. 8671-8678
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Hurley, J.H.1
Dean, A.M.2
Koshland, D.E.3
Stroud, R.M.4
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39
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0029940466
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Combining Laue diffraction and molecular dynamics to study enzyme intermediates
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Stoddard BL, Dean A, Bash PA. Combining Laue diffraction and molecular dynamics to study enzyme intermediates. Nat Struct Biol. 3:1996;590-595.
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(1996)
Nat Struct Biol
, vol.3
, pp. 590-595
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Stoddard, B.L.1
Dean, A.2
Bash, P.A.3
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41
-
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0032502775
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Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (αD60N) tryptophan synthase α2β2 complex reveals the correct orientation of active site αglu49
-
of outstanding interest. The structure of the enzyme tryptophan synthase was determined bound to its true substrate and compared to a previously determined structure complexed with the inhibitor indole-3-propanol phosphate. In the inhibitor-bound structure, the sidechain of αGlu49 is too distant to play a catalytic role in turnover. In the trapped ES complex, an induced-fit conformational change is observed that results in the movement and extension of that residue, allowing interaction with the 3-hydroxyl group of the substrate, as proposed from prior mechanistic studies. The results of this paper demonstrate how productive substrate complexes, determined using time-resolved methods, can provide structural detail missing from inhibitor complexes.
-
Rhee S, Miles EW, Davies DR. Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (αD60N) tryptophan synthase α2β2 complex reveals the correct orientation of active site αGlu49. of outstanding interest J Biol Chem. 273:1998;8553-8555 The structure of the enzyme tryptophan synthase was determined bound to its true substrate and compared to a previously determined structure complexed with the inhibitor indole-3-propanol phosphate. In the inhibitor-bound structure, the sidechain of αGlu49 is too distant to play a catalytic role in turnover. In the trapped ES complex, an induced-fit conformational change is observed that results in the movement and extension of that residue, allowing interaction with the 3-hydroxyl group of the substrate, as proposed from prior mechanistic studies. The results of this paper demonstrate how productive substrate complexes, determined using time-resolved methods, can provide structural detail missing from inhibitor complexes.
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(1998)
J Biol Chem
, vol.273
, pp. 8553-8555
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Rhee, S.1
Miles, E.W.2
Davies, D.R.3
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42
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0032554651
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Loop closure and intersubunit communication in tryptophan synthase
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of outstanding interest. A separate study on the same enzyme was reported in which an aminoacrylate intermediate of the β reaction was generated in the crystal under steady-state conditions using a flow cell. On the basis of these structures and many others, a pathway for communication between the α and β active sites is porposed.
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Schneider TR, Gerhardt E, Lee M, Liang P-H, Anderson KS, Schlichting I. Loop closure and intersubunit communication in tryptophan synthase. of outstanding interest Biochemistry. 37:1998;5394-5406 A separate study on the same enzyme was reported in which an aminoacrylate intermediate of the β reaction was generated in the crystal under steady-state conditions using a flow cell. On the basis of these structures and many others, a pathway for communication between the α and β active sites is porposed.
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(1998)
Biochemistry
, vol.37
, pp. 5394-5406
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Schneider, T.R.1
Gerhardt, E.2
Lee, M.3
Liang P-H4
Anderson, K.S.5
Schlichting, I.6
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43
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0028773124
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Laue diffraction study on the structure of cytochrome c peroxidase compound I
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Fulop V, Phizackerly RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL. Laue diffraction study on the structure of cytochrome c peroxidase compound I. Structure. 2:1994;201-208.
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(1994)
Structure
, vol.2
, pp. 201-208
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Fulop, V.1
Phizackerly, R.P.2
Soltis, S.M.3
Clifton, I.J.4
Wakatsuki, S.5
Erman, J.6
Hajdu, J.7
Edwards, S.L.8
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44
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0029859337
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Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy
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Gouet P, Jouve H-M, Williams PA, Andersson I, Andreoletti P, Nussaume L, Hajdu J. Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy. Nat Struct Biol. 3:1996;951-956.
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(1996)
Nat Struct Biol
, vol.3
, pp. 951-956
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Gouet, P.1
Jouve H-M2
Williams, P.A.3
Andersson, I.4
Andreoletti, P.5
Nussaume, L.6
Hajdu, J.7
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45
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0031453084
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Structural analysis of compound I in hemoproteins: Study on Proteus mirabilis catalase
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of special interest. This recent review compares time-resolved studies on the oxy-ferryl intermediates formed by cytochrome c peroxidase and Proteus mirabilis catalase, conducted using chemical trapping, and Laue or Weissenberg diffraction, respectively. The use of single-crystal microspectrophotometry in these studies is a particular strength of this work.
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Jouve HM, Andreoletti P, Gouet P, Hajdu J, Gagnon J. Structural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase. of special interest Biochimie. 79:1997;667-671 This recent review compares time-resolved studies on the oxy-ferryl intermediates formed by cytochrome c peroxidase and Proteus mirabilis catalase, conducted using chemical trapping, and Laue or Weissenberg diffraction, respectively. The use of single-crystal microspectrophotometry in these studies is a particular strength of this work.
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(1997)
Biochimie
, vol.79
, pp. 667-671
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Jouve, H.M.1
Andreoletti, P.2
Gouet, P.3
Hajdu, J.4
Gagnon, J.5
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46
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0002309181
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On the limitations of the Laue method when applied to crystals of macromolecules
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D. Moras, A.D. Podjarny, Thierry J.C. New York: Oxford University Press
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Hajdu J, Almo SC, Farber GK, Petsko GA, Wakatsuki S, Clifton IJ, Fulop V. On the limitations of the Laue method when applied to crystals of macromolecules. Moras D, Podjarny AD, Thierry JC. Crystallographic Computing. 1991;29-49 Oxford University Press, New York.
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(1991)
Crystallographic Computing
, pp. 29-49
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Hajdu, J.1
Almo, S.C.2
Farber, G.K.3
Petsko, G.A.4
Wakatsuki, S.5
Clifton, I.J.6
Fulop, V.7
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47
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0030852352
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Evaluation of Laue diffraction patterns
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of outstanding interest. C. Carter, Sweet R.M. Academic Press, San Diego, This review of the various algorithms and computational packages for Laue diffraction, including LAUEVIEW, LEAP and LAUEGEN, is a must-read for any aficionado of time-resolved crystallographic studies using polychromatic diffraction
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Clifton IJ, Duke EMH, Wakatsuki S, Ren Z. Evaluation of Laue diffraction patterns. of outstanding interest Carter C, Sweet RM. Methods in Enzymology. 1997;448-467 Academic Press, San Diego, This review of the various algorithms and computational packages for Laue diffraction, including LAUEVIEW, LEAP and LAUEGEN, is a must-read for any aficionado of time-resolved crystallographic studies using polychromatic diffraction.
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(1997)
Methods in Enzymology
, pp. 448-467
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Clifton, I.J.1
Duke, E.M.H.2
Wakatsuki, S.3
Ren, Z.4
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48
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0030947235
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Femtosecond time resolution in X-ray diffraction experiments
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of outstanding interest. The authors present a theoretical background for a method of femtosecond spectroscopy and X-ray diffraction, using extremely rapid laser pulses and topographic X-ray diffraction, to resolve diffraction profiles during the propagation of the excitation event through the crystal. A general treatment of the excitation and diffraction geometries in relation to spatial and temporal resolution is presented.
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Neutze R, Hadju J. Femtosecond time resolution in X-ray diffraction experiments. of outstanding interest Proc Natl Acad Sci USA. 94:1997;5651-5655 The authors present a theoretical background for a method of femtosecond spectroscopy and X-ray diffraction, using extremely rapid laser pulses and topographic X-ray diffraction, to resolve diffraction profiles during the propagation of the excitation event through the crystal. A general treatment of the excitation and diffraction geometries in relation to spatial and temporal resolution is presented.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 5651-5655
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Neutze, R.1
Hadju, J.2
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