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International Tables for Crystallography (2012). Vol. F. ch. 21.1, pp. 649-661
https://doi.org/10.1107/97809553602060000879 |
Chapter 21.1. Validation of protein crystal structures
Contents
- 21.1. Validation of protein crystal structures (pp. 649-661) | html | pdf | chapter contents |
- 21.1.1. Introduction (p. 649) | html | pdf |
- 21.1.2. Types of error (pp. 649-650) | html | pdf |
- 21.1.3. Detecting outliers (pp. 650-651) | html | pdf |
- 21.1.4. Fixing errors (pp. 651-652) | html | pdf |
- 21.1.5. Preventing errors (p. 652) | html | pdf |
- 21.1.6. Final model (p. 652) | html | pdf |
- 21.1.7. A compendium of quality criteria (pp. 652-658) | html | pdf |
- 21.1.7.1. Data quality (pp. 653-654) | html | pdf |
- 21.1.7.1.1. Merging R values (p. 653) | html | pdf |
- 21.1.7.1.2. Completeness (p. 653) | html | pdf |
- 21.1.7.1.3. Redundancy (p. 653) | html | pdf |
- 21.1.7.1.4. Signal strength (p. 653) | html | pdf |
- 21.1.7.1.5. Resolution (p. 653) | html | pdf |
- 21.1.7.1.6. Unit-cell parameters (pp. 653-654) | html | pdf |
- 21.1.7.1.7. Symmetry (p. 654) | html | pdf |
- 21.1.7.2. Model quality, coordinates (pp. 654-656) | html | pdf |
- 21.1.7.2.1. Geometry and stereochemistry (p. 654) | html | pdf |
- 21.1.7.2.2. Torsion angles (dihedrals) (pp. 654-655) | html | pdf |
- 21.1.7.2.3. Cα-only models (p. 655) | html | pdf |
- 21.1.7.2.4. Contacts and environments (pp. 655-656) | html | pdf |
- 21.1.7.2.5. Noncrystallographic symmetry (p. 656) | html | pdf |
- 21.1.7.2.6. Solvent molecules (p. 656) | html | pdf |
- 21.1.7.2.7. Miscellaneous (p. 656) | html | pdf |
- 21.1.7.3. Model quality, temperature factors (pp. 656-657) | html | pdf |
- 21.1.7.4. Model versus experimental data (pp. 657-658) | html | pdf |
- 21.1.7.5. Accountancy (p. 658) | html | pdf |
- 21.1.7.1. Data quality (pp. 653-654) | html | pdf |
- 21.1.8. Future (p. 658) | html | pdf |
- References | html | pdf |