International Tables for Crystallography (2012). Vol. F, ch. 4.1, pp. 99-121   | 1 | 2 |
doi: 10.1107/97809553602060000812

Chapter 4.1. General methods

Contents

  • 4.1. General methods  (pp. 99-121) | html | pdf | chapter contents |
    • 4.1.1. Introduction  (pp. 99-100) | html | pdf |
      • 4.1.1.1. Prologue  (p. 99) | html | pdf |
      • 4.1.1.2. Crystallization principles  (pp. 99-100) | html | pdf |
    • 4.1.2. Main parameters that affect crystallization of macromolecules  (pp. 100-104) | html | pdf |
      • 4.1.2.1. Crystallizing agents  (pp. 100-101) | html | pdf |
      • 4.1.2.2. Physical, physical–chemical and biochemical variables  (pp. 101-102) | html | pdf |
      • 4.1.2.3. Additives  (pp. 102-103) | html | pdf |
      • 4.1.2.4. Purity and homogeneity  (pp. 103-104) | html | pdf |
    • 4.1.3. Crystallization arrangements and classical methodologies  (pp. 104-107) | html | pdf |
      • 4.1.3.1. Historical development of methods  (pp. 104-105) | html | pdf |
      • 4.1.3.2. Batch crystallizations  (p. 105) | html | pdf |
      • 4.1.3.3. Dialysis methods  (p. 105) | html | pdf |
      • 4.1.3.4. Vapour-diffusion methods  (p. 106) | html | pdf |
      • 4.1.3.5. Free-interface and counter-diffusion methods  (p. 107) | html | pdf |
      • 4.1.3.6. Miniaturization, automation and robotics  (p. 107) | html | pdf |
    • 4.1.4. Advanced crystallization methodologies  (pp. 107-111) | html | pdf |
      • 4.1.4.1. Crystallization in convection-free media  (pp. 107-110) | html | pdf |
      • 4.1.4.2. Methods making use of temperature and pressure  (p. 110) | html | pdf |
      • 4.1.4.3. Methods making use of crystallization chaperones  (p. 110) | html | pdf |
      • 4.1.4.4. Seeding  (pp. 110-111) | html | pdf |
    • 4.1.5. From the macromolecule to perfect crystals: the physics view  (pp. 111-113) | html | pdf |
      • 4.1.5.1. Prenucleation and nucleation  (p. 111) | html | pdf |
      • 4.1.5.2. Growth and cessation of growth  (pp. 111-112) | html | pdf |
      • 4.1.5.3. Uncoupling nucleation and growth, and the constant-growth regime  (p. 112) | html | pdf |
      • 4.1.5.4. Crystal perfection  (pp. 112-113) | html | pdf |
    • 4.1.6. How to crystallize a new macromolecule: the structural biology view  (pp. 113-115) | html | pdf |
      • 4.1.6.1. How to start and how to choose what screening kits to start with  (p. 113) | html | pdf |
      • 4.1.6.2. Rules and general principles  (p. 114) | html | pdf |
      • 4.1.6.3. Database mining and statistics  (pp. 114-115) | html | pdf |
      • 4.1.6.4. Strategic concerns: a summary  (p. 115) | html | pdf |
    • 4.1.7. The future of protein crystal growth  (p. 115) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 4.1.1.1. Crystallization is a multiparametric process under the control of a great variety of biochemical, chemical and physical parameters  (p. 100) | html | pdf |
      • Fig. 4.1.3.1. Principles of major methods used to crystallize biological macromolecules  (p. 104) | html | pdf |
      • Fig. 4.1.3.2. The evolution of crystallization plates from hand-made assays to the high-throughput era  (p. 105) | html | pdf |
      • Fig. 4.1.4.1. Examples of microfluidic devices designed for biocrystallization  (p. 109) | html | pdf |
      • Fig. 4.1.5.1. Growth mechanisms and visualization of protein crystal surfaces by AFM  (p. 112) | html | pdf |
      • Fig. 4.1.6.1. From the target molecule to its three-dimensional structure: a flowchart for a structure detemination  (p. 113) | html | pdf |