International Tables for Crystallography (2012). Vol. F, ch. 3.1, pp. 75-91   | 1 | 2 |
doi: 10.1107/97809553602060000810

Chapter 3.1. Preparing recombinant proteins for X-ray crystallography

Contents

  • 3.1. Preparing recombinant proteins for X-ray crystallography  (pp. 75-91) | html | pdf | chapter contents |
    • 3.1.1. Introduction  (p. 75) | html | pdf |
    • 3.1.2. Overview  (pp. 75-76) | html | pdf |
    • 3.1.3. Engineering an expression construct  (pp. 76-77) | html | pdf |
      • 3.1.3.1. Choosing an expression system  (p. 76) | html | pdf |
      • 3.1.3.2. Creating an expression construct  (pp. 76-77) | html | pdf |
      • 3.1.3.3. Addition of tags or domains  (p. 77) | html | pdf |
    • 3.1.4. Expression systems  (pp. 77-85) | html | pdf |
      • 3.1.4.1. E. coli   (pp. 77-82) | html | pdf |
      • 3.1.4.2. Yeast  (pp. 82-83) | html | pdf |
      • 3.1.4.3. Baculoviruses and insect cells  (pp. 83-84) | html | pdf |
      • 3.1.4.4. Mammalian cells  (pp. 84-85) | html | pdf |
    • 3.1.5. Protein purification  (pp. 85-88) | html | pdf |
      • 3.1.5.1. Conventional protein purification  (pp. 85-87) | html | pdf |
      • 3.1.5.2. Affinity purification  (p. 87) | html | pdf |
      • 3.1.5.3. Purifying and refolding denatured proteins  (pp. 87-88) | html | pdf |
    • 3.1.6. Characterization of the purified product  (pp. 88-89) | html | pdf |
      • 3.1.6.1. Assessment of sample homogeneity  (pp. 88-89) | html | pdf |
      • 3.1.6.2. Protein storage  (p. 89) | html | pdf |
    • 3.1.7. Reprise  (pp. 89-90) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 3.1.3.1. Creating an expression construct  (p. 77) | html | pdf |
      • Fig. 3.1.5.1. Protein purification strategy  (p. 86) | html | pdf |
    • Tables
      • Table 3.1.4.1. Strategies for improving expression in E. coli   (p. 79) | html | pdf |