International Tables for Crystallography (2006). Vol. F, ch. 19.2, pp. 423-427   | 1 | 2 |
doi: 10.1107/97809553602060000699

Chapter 19.2. Electron diffraction of protein crystals

Contents

  • 19.2. Electron diffraction of protein crystals  (pp. 423-427) | html | pdf | chapter contents |
    • 19.2.1. Electron scattering  (p. 423) | html | pdf |
    • 19.2.2. The electron microscope  (p. 423) | html | pdf |
    • 19.2.3. Data collection  (pp. 423-424) | html | pdf |
      • 19.2.3.1. Specimen preparation  (p. 423) | html | pdf |
      • 19.2.3.2. Radiation damage  (p. 424) | html | pdf |
      • 19.2.3.3. Other technical factors  (p. 424) | html | pdf |
    • 19.2.4. Data processing  (pp. 425-427) | html | pdf |
      • 19.2.4.1. Data sampling  (pp. 425-426) | html | pdf |
      • 19.2.4.2. Amplitudes and phases  (pp. 426-427) | html | pdf |
      • 19.2.4.3. 3D map  (p. 427) | html | pdf |
      • 19.2.4.4. Refinement  (p. 427) | html | pdf |
    • 19.2.5. Future development  (p. 427) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 19.2.3.1. Electron diffraction pattern of trehalose-embedded bacteriorhodopsin, with Bragg reflections extending to 2.5 Å  (p. 424) | html | pdf |
      • Fig. 19.2.4.1. Schematic diagram of data distribution in Fourier space for a two-dimensional crystal  (p. 424) | html | pdf |
      • Fig. 19.2.4.2. Experimental intensities from electron diffraction patterns and phases from images of bacteriorhodopsin, recorded from tilted crystals in an electron cryomicroscope  (p. 425) | html | pdf |
      • Fig. 19.2.4.3. Ribbon diagram of a tubulin dimer, whose structure has been solved to 3.7 Å resolution  (p. 426) | html | pdf |