International Tables for Crystallography (2012). Vol. F. ch. 1.2, pp. 5-12
https://doi.org/10.1107/97809553602060000805 |
Chapter 1.2. Historical background
Contents
- 1.2. Historical background (pp. 5-12) | html | pdf | chapter contents |
- 1.2.1. Introduction (p. 5) | html | pdf |
- 1.2.2. 1912 to the 1950s (pp. 5-6) | html | pdf |
- 1.2.3. The first investigations of biological macromolecules (pp. 6-7) | html | pdf |
- 1.2.4. Globular proteins in the 1950s (pp. 7-8) | html | pdf |
- 1.2.5. The first protein structures (1957 to the 1970s) (pp. 8-9) | html | pdf |
- 1.2.6. Technological developments (1958 to the 1980s) (pp. 9-10) | html | pdf |
- 1.2.7. Meetings (p. 10) | 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 h0l reflections at various lattice shrinkage stages (C, C′, D, E, F, G, H, J) (p. 7) | html | pdf |
- Fig. 1.2.5.1. A model of the myoglobin molecule at 6 Å resolution (p. 8) | html | pdf |
- Fig. 1.2.5.2. Cylindrical sections through a helical segment of a myoglobin polypeptide chain (p. 8) | 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. 10) | html | pdf |