International Tables for Crystallography (2012). Vol. F, ch. 3.2, pp. 92-98
doi: 10.1107/97809553602060000811

Chapter 3.2. Expression and purification of membrane proteins for structural studies

Contents

  • 3.2. Expression and purification of membrane proteins for structural studies  (pp. 92-98) | html | pdf | chapter contents |
    • 3.2.1. Introduction  (p. 92) | html | pdf |
    • 3.2.2. A consensus strategy for membrane-protein expression  (pp. 92-93) | html | pdf |
      • 3.2.2.1. Choosing the expression system and affinity tags  (p. 92) | html | pdf |
      • 3.2.2.2. Strategies for improving membrane-protein expression  (p. 93) | html | pdf |
    • 3.2.3. A consensus strategy for membrane-protein purification  (pp. 93-96) | html | pdf |
      • 3.2.3.1. General principles  (pp. 93-94) | html | pdf |
      • 3.2.3.2. Cell lysis and membrane isolation  (p. 94) | html | pdf |
      • 3.2.3.3. Detergent extraction of membrane proteins  (pp. 94-95) | html | pdf |
      • 3.2.3.4. General considerations for monitoring membrane-protein activity  (p. 95) | html | pdf |
      • 3.2.3.5. Primary purification: affinity chromatography  (p. 95) | html | pdf |
      • 3.2.3.6. Secondary purification: size-exclusion and ion-exchange chromatography  (p. 95) | html | pdf |
      • 3.2.3.7. Concentrating membrane-protein samples for crystallography  (pp. 95-96) | html | pdf |
    • 3.2.4. Common purification pitfalls and prioritized alternative strategies  (p. 96) | html | pdf |
      • 3.2.4.1. Poor solubility of the target protein  (p. 96) | html | pdf |
      • 3.2.4.2. The isolated target protein does not crystallize  (p. 96) | html | pdf |
    • 3.2.5. Summary  (p. 96) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 3.2.3.1. Flow diagram of the membrane-protein purification strategy  (p. 94) | html | pdf |
    • Tables
      • Table 3.2.2.1. Strategies for improving recombinant membrane-protein expression in E. coli   (p. 93) | html | pdf |