International Tables for Crystallography (2006). Vol. F. ch. 24.4, pp. 669-674   | 1 | 2 |
https://doi.org/10.1107/97809553602060000721

Chapter 24.4. The Biological Macromolecule Crystallization Database

Contents

  • 24.4. The Biological Macromolecule Crystallization Database  (pp. 669-674) | html | pdf | chapter contents |
    G. L. Gilliland, M. Tung and J. E. Ladner
    • 24.4.1. Introduction  (p. 669) | html | pdf |
    • 24.4.2. History of the BMCD  (p. 669) | html | pdf |
    • 24.4.3. BMCD data  (p. 669) | html | pdf |
    • 24.4.4. BMCD implementation – web interface  (p. 670) | html | pdf |
    • 24.4.5. Reproducing published crystallization procedures  (pp. 670-671) | html | pdf |
    • 24.4.6. Crystallization screens  (p. 671) | html | pdf |
    • 24.4.7. A general crystallization procedure  (pp. 671-674) | html | pdf |
    • 24.4.8. The future of the BMCD  (p. 674) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 24.4.3.1. A representative example of a biological macromolecule, subtilisin BPN′: prodomain, entry M1MT in the BMCD  (p. 670) | html | pdf |
      • Fig. 24.4.3.2. A representative example of a crystal entry C2CK for the subtilsin BPN′: prodomain, entry M1MT in the BMCD  (p. 670) | html | pdf |
      • Fig. 24.4.5.1. Crystal of recombinant rat liver glutathione S-transferase (Ji et al  (p. 671) | html | pdf |
      • Fig. 24.4.7.1. A general crystallization strategy based on the data contained in the BMCD  (p. 671) | html | pdf |
    • Tables
      • Table 24.4.6.1. Crystallization conditions for endonucleases  (pp. 672-673) | html | pdf |