International Tables for Crystallography (2006). Vol. F. ch. 18.4, pp. 393-402
https://doi.org/10.1107/97809553602060000696 |
Chapter 18.4. Refinement at atomic resolution
Contents
- 18.4. Refinement at atomic resolution (pp. 393-402) | html | pdf | chapter contents |
- 18.4.1. Definition of atomic resolution (pp. 393-395) | html | pdf |
- 18.4.2. Data (p. 395) | html | pdf |
- 18.4.3. Computational algorithms and strategies (p. 396) | html | pdf |
- 18.4.3.1. Classical least-squares refinement of small molecules (p. 396) | html | pdf |
- 18.4.3.2. Least-squares refinement of large structures (p. 396) | html | pdf |
- 18.4.3.3. Fast Fourier transform (p. 396) | html | pdf |
- 18.4.3.4. Maximum likelihood (p. 396) | html | pdf |
- 18.4.3.5. Computer power (p. 396) | html | pdf |
- 18.4.4. Computational options and tactics (pp. 396-398) | html | pdf |
- 18.4.4.1. Use of F or F2 (pp. 396-397) | html | pdf |
- 18.4.4.2. Restraints and/or constraints on coordinates and ADPs (p. 397) | html | pdf |
- 18.4.4.3. Partial occupancy (p. 397) | html | pdf |
- 18.4.4.4. Validation of extra parameters during the refinement process (pp. 397-398) | html | pdf |
- 18.4.4.5. Practical strategies (p. 398) | html | pdf |
- 18.4.5. Features in the refined model (pp. 398-401) | html | pdf |
- 18.4.5.1. Hydrogen atoms (pp. 398-399) | html | pdf |
- 18.4.5.2. Anisotropic atomic displacement parameters (p. 399) | html | pdf |
- 18.4.5.3. Alternative conformations (p. 399) | html | pdf |
- 18.4.5.4. Ordered solvent water (pp. 399-400) | html | pdf |
- 18.4.5.5. Automatic location of water sites (p. 400) | html | pdf |
- 18.4.5.6. Bulk solvent and the low-resolution reflections (pp. 400-401) | html | pdf |
- 18.4.5.7. Metal ions and other ligands in the solvent (p. 401) | html | pdf |
- 18.4.5.8. Deformation density (p. 401) | html | pdf |
- 18.4.6. Quality assessment of the model (p. 401) | html | pdf |
- 18.4.7. Relation to biological chemistry (pp. 401-402) | html | pdf |
- References | html | pdf |
- Figures
- Fig. 18.4.1.1. The thermal-ellipsoid model used to represent anisotropic atomic displacement, with major axes indicated (p. 393) | html | pdf |
- Fig. 18.4.1.2. Histograms of B values for a protein structure, Micrococcus lysodecticus catalase (Murshudov et al (p. 394) | html | pdf |
- Fig. 18.4.5.1. (a), (b) Representative electron-density maps for the refinement of Clostridium acidurici ferredoxin at 0.94 Å resolution (Dauter, Wilson et al (p. 398) | html | pdf |
- Fig. 18.4.5.2. Schematic representation of the bulk-solvent models described in the text (p. 400) | html | pdf |
- Tables