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Synchrotron radiation, using a beam size of 10 μm, has made possible the diffraction of single fibers of silk, rather than the bundles used in earlier work. Diffraction of single fibers allows the study of orientation distributions and fiber texture.
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A spider was persuaded to produce a silk fiber for eight hours continuously at a synchrotron X-ray microbeam (7 μm diameter) for diffraction. Single fibers could thus be used to study the formation of the fiber orientation and crystallinity.
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Six different amyloid fibrils and two synthetic polypeptides gave similar high-resolution diffraction patterns. The authors postulate a structure consisting of a helical array of β sheets stacked parallel to the fiber axis.
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Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol. 273:1997;729-739. Six different amyloid fibrils and two synthetic polypeptides gave similar high-resolution diffraction patterns. The authors postulate a structure consisting of a helical array of β sheets stacked parallel to the fiber axis.
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Fiber diffraction of N-terminal peptides of Alzheimer's disease β-amyloid fibrils shows a cross-β structure, consistent with tubular, 30 Å diameter protofilaments. The birefringence of solutions was used to predict the capacity for magnetic orientation.
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High-resolution neutron fiber diffraction was used to identify and refine the positions and occupancies of water molecules in DNA. A central core of water runs along the axis of the double helix and chains of ordered water lie in the center of the major groove.
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A structural study primarily of interest to DNA chemists; however, this paper also includes an extensive description of methods, including a synchrotron X-ray fiber diffraction camera, sample holder and data collection systems.
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Pope LH, Shotton MW, Forsyth T, Hughes DJ, Denny RC, Fuller W Structural polymorphism in a tubercidin analogue of the DNA double helix. Biophys Chem. 70:1998;161-172. A structural study primarily of interest to DNA chemists; however, this paper also includes an extensive description of methods, including a synchrotron X-ray fiber diffraction camera, sample holder and data collection systems.
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Structure of ribgrass mosaic virus at 2.9 Å resolution. Evolution and taxonomy of tobamoviruses
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The most reliable yet in a series of fiber diffraction structure determinations of tobamoviruses. The ribgrass mosaic virus structure was determined from that of tobacco mosaic virus and refined by molecular dynamics to an R factor of 0.095
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Wang H, Culver JN, Stubbs G Structure of ribgrass mosaic virus at 2.9 Å resolution. Evolution and taxonomy of tobamoviruses. J Mol Biol. 269:1997;769-779. The most reliable yet in a series of fiber diffraction structure determinations of tobamoviruses. The ribgrass mosaic virus structure was determined from that of tobacco mosaic virus and refined by molecular dynamics to an R factor of 0.095.
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Structure of the capsid of Pf3 filamentous phage determined from X-ray fiber diffraction data at 3.1 Å resolution
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The capsid of the Pf3 filamentous phage has a similar structure to that of Pf1, despite large differences in their protein sequence and DNA packaging. Magnetic alignment, simulated annealing refinement and free R factor measurements were all used.
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Welsh LC, Symmons MF, Sturtevant JM, Marvin DA, Perham RN Structure of the capsid of Pf3 filamentous phage determined from X-ray fiber diffraction data at 3.1 Å resolution. J Mol Biol. 283:1998;155-177. The capsid of the Pf3 filamentous phage has a similar structure to that of Pf1, despite large differences in their protein sequence and DNA packaging. Magnetic alignment, simulated annealing refinement and free R factor measurements were all used.
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Multiple-step method for making exceptionally well-oriented liquid-crystalline sols of macromolecular assemblies
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A detailed description of a procedure using centrifugation and magnets to align flagellar filaments in solution to disorientations of only 0.6°. Breathtaking diffraction patterns are presented! Essential reading for anyone wanting to make better oriented sols.
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Yamashita I, Suzuki H, Namba K Multiple-step method for making exceptionally well-oriented liquid-crystalline sols of macromolecular assemblies. J Mol Biol. 278:1998;609-615. A detailed description of a procedure using centrifugation and magnets to align flagellar filaments in solution to disorientations of only 0.6°. Breathtaking diffraction patterns are presented! Essential reading for anyone wanting to make better oriented sols.
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This application of the methods developed for orienting flagella shows that not all filaments align under the same or even the expected conditions. Excellent diffraction patterns to 6 Å resolution are shown.
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The susceptibility of pure tubulin to high magnetic fields: A magnetic birefringence and X-ray fiber diffraction study
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Microtubules are extremely difficult to handle. A description of the most careful and systematic study yet of the effect of high magnetic fields on tubulin during its assembly to form microtubules.
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Myosin head configuration in relaxed fish muscle: Resting state myosin heads must swing axially by up to 150 Å or turn upside down to reach rigor
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This paper presents the low-resolution structure of relaxed muscle, especially the myosin head configuration. Time-resolved synchrotron diffraction, simulated annealing during initial model building and free R factor measurements are involved.
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The study of myosin interactions with actin during muscle contraction. Individual reflection intensity was used as a probe of structural state. Synchrotron radiation allowed time-resolved studies (1 ms exposures), even though the experiments required the use of very small specimens (single muscle fibers).
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An excellent description of the instrumentation, data collection and early stages of data processing at the Daresbury (UK) synchrotron and Institute Laue Langevin (France) neutron source.
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Shotton MW, Pope LH, Forsyth VT, Denny RC, Archer J, Langan P, Ye H, Boote C New developments in instrumentation for X-ray and neutron fiber diffraction experiments. J Appl Crystallogr. 31:1998;758-766. An excellent description of the instrumentation, data collection and early stages of data processing at the Daresbury (UK) synchrotron and Institute Laue Langevin (France) neutron source.
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