International Tables for Crystallography (2012). Vol. F, ch. 8.1, pp. 189-204   | 1 | 2 |
doi: 10.1107/97809553602060000822

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

Contents

  • 8.1. Synchrotron-radiation instrumentation, methods and scientific utilization  (pp. 189-204) | html | pdf | chapter contents |
    • 8.1.1. Introduction  (p. 189) | html | pdf |
    • 8.1.2. The physics of SR  (pp. 189-190) | html | pdf |
    • 8.1.3. Insertion devices (IDs)  (pp. 190-191) | html | pdf |
    • 8.1.4. Beam characteristics delivered at the crystal sample  (pp. 191-192) | html | pdf |
    • 8.1.5. Evolution of SR machines and experiments  (pp. 192-194) | html | pdf |
      • 8.1.5.1. First-generation SR machines  (pp. 192-193) | html | pdf |
      • 8.1.5.2. Second-generation dedicated machines  (p. 193) | html | pdf |
      • 8.1.5.3. Third-generation high spectral brightness machines  (pp. 193-194) | html | pdf |
      • 8.1.5.4. New national SR machines  (p. 194) | html | pdf |
      • 8.1.5.5. X-ray free-electron lasers (XFELs)  (p. 194) | html | pdf |
    • 8.1.6. SR instrumentation  (pp. 194-195) | html | pdf |
    • 8.1.7. SR monochromatic and Laue diffraction geometry  (pp. 195-197) | html | pdf |
      • 8.1.7.1. Laue geometry: sources, optics, sample reflection bandwidth and spot size  (pp. 195-196) | html | pdf |
      • 8.1.7.2. Monochromatic SR beams: optical configurations and sample rocking width  (pp. 196-197) | html | pdf |
        • 8.1.7.2.1. Curved single-crystal monochromator  (p. 196) | html | pdf |
        • 8.1.7.2.2. Double-crystal monochromator  (p. 196) | html | pdf |
        • 8.1.7.2.3. Widening of monochromatic wavelength range provision  (pp. 196-197) | html | pdf |
        • 8.1.7.2.4. Crystal sample rocking width  (p. 197) | html | pdf |
    • 8.1.8. Scientific utilization of SR in protein crystallography  (pp. 197-200) | html | pdf |
      • 8.1.8.1. Atomic and ultra-high-resolution macromolecular crystallography  (p. 198) | html | pdf |
      • 8.1.8.2. Small crystals  (p. 198) | html | pdf |
      • 8.1.8.3. Time-resolved macromolecular crystallography  (p. 198) | html | pdf |
      • 8.1.8.4. Multi-macromolecular complexes  (pp. 198-199) | html | pdf |
      • 8.1.8.5. Optimized anomalous dispersion (MAD), improved multiple isomorphous replacement (MIR) data and `structural genomics'   (pp. 199-200) | html | pdf |
      • 8.1.8.6. Radiation damage  (p. 200) | html | pdf |
    • 8.1.9. Concluding remarks  (p. 200) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 8.1.2.1. The ring tunnel and part of the machine lattice at the ESRF, Grenoble, France  (p. 189) | html | pdf |
      • Fig. 8.1.2.2. SR spectra  (p. 190) | html | pdf |
      • Fig. 8.1.4.1. Common beamline optics modes  (p. 191) | html | pdf |
      • Fig. 8.1.4.2. Single-crystal SR diffraction patterns  (p. 191) | html | pdf |
      • Fig. 8.1.5.1. Anomalous dispersion  (p. 193) | html | pdf |
      • Fig. 8.1.7.1. Single-crystal monochromator illuminated by SR  (p. 196) | html | pdf |
      • Fig. 8.1.7.2. Double-crystal monochromator illuminated by SR  (p. 197) | 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. 197) | 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. 198) | html | pdf |
      • Fig. 8.1.8.2. A view of SV40 virus  (p. 199) | html | pdf |
      • Fig. 8.1.8.3. The protein crystal structure of F 1 ATPase  (p. 199) | html | pdf |
      • Fig. 8.1.8.4. Side view of the structure of Photosystem II, the water-splitting enzyme of photosynthesis, determined using X-ray crystallography based on data recorded at the SLS and ESRF  (p. 199) | html | pdf |
      • Fig. 8.1.9.1. Synchrotron structures deposited in the PDB versus all PDB deposited structures  (p. 200) | html | pdf |
    • Tables
      • Table 8.1.4.1. Internet addresses of SR facilities with macromolecular crystallography beamlines  (p. 192) | html | pdf |
      • Table 8.1.5.1. Structures in the Protein Data Bank (PDB) for which data were collected at the SRS  (p. 194) | html | pdf |