International Tables for Crystallography (2006). Vol. F, ch. 1.2, pp. 4-9   | 1 | 2 |
doi: 10.1107/97809553602060000655

Chapter 1.2. Historical background

Contents

  • 1.2. Historical background  (pp. 4-9) | html | pdf | chapter contents |
    • 1.2.1. Introduction  (p. 4) | html | pdf |
    • 1.2.2. 1912 to the 1950s  (pp. 4-5) | html | pdf |
    • 1.2.3. The first investigations of biological macromolecules  (p. 5) | html | pdf |
    • 1.2.4. Globular proteins in the 1950s  (pp. 5-7) | html | pdf |
    • 1.2.5. The first protein structures (1957 to the 1970s)  (pp. 7-8) | html | pdf |
    • 1.2.6. Technological developments (1958 to the 1980s)  (pp. 8-9) | html | pdf |
    • 1.2.7. Meetings  (p. 9) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 1.2.4.1. Change of structure amplitude for horse haemoglobin as a function of salt concentration in the suspension medium of the low-order h 0 l reflections at various lattice shrinkage stages (C, C′, D, E, F, G, H, J)  (p. 6) | html | pdf |
      • Fig. 1.2.5.1. A model of the myoglobin molecule at 6 Å resolution  (p. 7) | html | pdf |
      • Fig. 1.2.5.2. Cylindrical sections through a helical segment of a myoglobin polypeptide chain  (p. 7) | html | pdf |
      • Fig. 1.2.6.1. The 2 Å-resolution map of sperm-whale myoglobin was represented by coloured Meccano-set clips on a forest of vertical rods  (p. 8) | html | pdf |