International Tables for Crystallography (2006). Vol. F, ch. 3.1, pp. 65-80   | 1 | 2 |
doi: 10.1107/97809553602060000659

Chapter 3.1. Preparing recombinant proteins for X-ray crystallography

Contents

  • 3.1. Preparing recombinant proteins for X-ray crystallography  (pp. 65-80) | html | pdf | chapter contents |
    • 3.1.1. Introduction  (p. 65) | html | pdf |
    • 3.1.2. Overview  (p. 65) | html | pdf |
    • 3.1.3. Engineering an expression construct  (pp. 66-67) | html | pdf |
      • 3.1.3.1. Choosing an expression system  (p. 66) | html | pdf |
      • 3.1.3.2. Creating an expression construct  (p. 66) | html | pdf |
      • 3.1.3.3. Addition of tags or domains  (p. 67) | html | pdf |
    • 3.1.4. Expression systems  (pp. 67-74) | html | pdf |
      • 3.1.4.1. E. coli   (pp. 67-71) | html | pdf |
      • 3.1.4.2. Yeast  (pp. 71-72) | html | pdf |
      • 3.1.4.3. Baculoviruses and insect cells  (pp. 72-73) | html | pdf |
      • 3.1.4.4. Mammalian cells  (pp. 73-74) | html | pdf |
    • 3.1.5. Protein purification  (pp. 75-77) | html | pdf |
      • 3.1.5.1. Conventional protein purification  (pp. 75-76) | html | pdf |
      • 3.1.5.2. Affinity purification  (pp. 76-77) | html | pdf |
      • 3.1.5.3. Purifying and refolding denatured proteins  (p. 77) | html | pdf |
    • 3.1.6. Characterization of the purified product  (pp. 77-78) | html | pdf |
      • 3.1.6.1. Assessment of sample homogeneity  (pp. 77-78) | html | pdf |
      • 3.1.6.2. Protein storage  (p. 78) | html | pdf |
    • 3.1.7. Reprise  (pp. 78-79) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 3.1.3.1. Creating an expression construct  (p. 67) | html | pdf |
      • Fig. 3.1.5.1. Protein purification strategy  (p. 75) | html | pdf |
    • Tables
      • Table 3.1.4.1. Strategies for improving expression in E. coli   (p. 68) | html | pdf |