International Tables for Crystallography (2006). Vol. F. ch. 8.1, pp. 155-166   | 1 | 2 |
https://doi.org/10.1107/97809553602060000669

Chapter 8.1. Synchrotron-radiation instrumentation, methods and scientific utilization

Contents

  • 8.1. Synchrotron-radiation instrumentation, methods and scientific utilization  (pp. 155-166) | html | pdf | chapter contents |
    J. R. Helliwell
    • 8.1.1. Introduction  (p. 155) | html | pdf |
    • 8.1.2. The physics of SR  (p. 155) | html | pdf |
    • 8.1.3. Insertion devices (IDs)  (pp. 155-156) | html | pdf |
    • 8.1.4. Beam characteristics delivered at the crystal sample  (pp. 156-158) | html | pdf |
    • 8.1.5. Evolution of SR machines and experiments  (pp. 158-161) | html | pdf |
      • 8.1.5.1. First-generation SR machines  (pp. 158-159) | html | pdf |
      • 8.1.5.2. Second-generation dedicated machines  (p. 160) | html | pdf |
      • 8.1.5.3. Third-generation high-brilliance machines  (pp. 160-161) | html | pdf |
      • 8.1.5.4. New national SR machines  (p. 161) | html | pdf |
      • 8.1.5.5. X-ray free electron laser (XFEL)  (p. 161) | html | pdf |
    • 8.1.6. SR instrumentation  (pp. 161-162) | html | pdf |
    • 8.1.7. SR monochromatic and Laue diffraction geometry  (pp. 162-164) | html | pdf |
      • 8.1.7.1. Laue geometry: sources, optics, sample reflection bandwidth and spot size  (p. 162) | html | pdf |
      • 8.1.7.2. Monochromatic SR beams: optical configurations and sample rocking width  (pp. 162-164) | html | pdf |
        • 8.1.7.2.1. Curved single-crystal monochromator  (pp. 162-163) | html | pdf |
        • 8.1.7.2.2. Double-crystal monochromator  (p. 163) | html | pdf |
        • 8.1.7.2.3. Crystal sample rocking width  (pp. 163-164) | html | pdf |
    • 8.1.8. Scientific utilization of SR in protein crystallography  (pp. 164-166) | html | pdf |
      • 8.1.8.1. Atomic and ultra high resolution macromolecular crystallography  (p. 165) | html | pdf |
      • 8.1.8.2. Small crystals  (p. 165) | html | pdf |
      • 8.1.8.3. Time-resolved macromolecular crystallography  (p. 165) | html | pdf |
      • 8.1.8.4. Multi-macromolecular complexes  (p. 165) | html | pdf |
      • 8.1.8.5. Optimized anomalous dispersion (MAD), improved MIR data and `structural genomics'   (pp. 165-166) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 8.1.2.1. (a) Evolution of X-ray source brilliance  (p. 156) | html | pdf |
      • Fig. 8.1.2.2. Overall layout of the Daresbury SRS facility  (p. 157) | html | pdf |
      • Fig. 8.1.2.3. The ring tunnel and part of the machine lattice at the ESRF, Grenoble, France  (p. 158) | html | pdf |
      • Fig. 8.1.2.4. SR spectra  (p. 158) | html | pdf |
      • Fig. 8.1.4.1. Common beamline optics modes  (p. 159) | html | pdf |
      • Fig. 8.1.4.2. Single-crystal SR diffraction patterns  (p. 159) | html | pdf |
      • Fig. 8.1.5.1. Anomalous dispersion  (p. 160) | html | pdf |
      • Fig. 8.1.7.1. Single-crystal monochromator illuminated by SR  (p. 163) | html | pdf |
      • Fig. 8.1.7.2. Double-crystal monochromator illuminated by SR  (p. 163) | html | pdf |
      • Fig. 8.1.7.3. The rocking width of an individual reflection for the case of Fig. 8.1.7.1(c) and a vertical rotation axis  (p. 164) | html | pdf |
      • Fig. 8.1.8.1. Determination of the protonation states of carboxylic acid side chains in proteins via hydrogen atoms and resolved single and double bond lengths  (p. 164) | html | pdf |
      • Fig. 8.1.8.2. A view of SV40 virus  (p. 164) | html | pdf |
      • Fig. 8.1.8.3. The protein crystal structure of F1 ATPase  (p. 164) | html | pdf |
    • Tables
      • Table 8.1.4.1. Internet addresses of SR facilities with macromolecular crystallography beamlines  (p. 157) | html | pdf |
      • Table 8.1.5.1. A comparison of the parameter list for the 2 GeV SRS, 1997, and the new higher-energy machine for the UK, DIAMOND  (p. 160) | html | pdf |