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International Tables for Crystallography (2006). Vol. F. ch. 21.1, pp. 497-506
https://doi.org/10.1107/97809553602060000707 |
Chapter 21.1. Validation of protein crystal structures
Contents
- 21.1. Validation of protein crystal structures (pp. 497-506) | html | pdf | chapter contents |
- 21.1.1. Introduction (p. 497) | html | pdf |
- 21.1.2. Types of error (pp. 497-498) | html | pdf |
- 21.1.3. Detecting outliers (pp. 498-499) | html | pdf |
- 21.1.4. Fixing errors (p. 499) | html | pdf |
- 21.1.5. Preventing errors (pp. 499-500) | html | pdf |
- 21.1.6. Final model (p. 500) | html | pdf |
- 21.1.7. A compendium of quality criteria (pp. 500-505) | html | pdf |
- 21.1.7.1. Data quality (pp. 500-501) | html | pdf |
- 21.1.7.1.1. Merging R values (pp. 500-501) | html | pdf |
- 21.1.7.1.2. Completeness (p. 501) | html | pdf |
- 21.1.7.1.3. Redundancy (p. 501) | html | pdf |
- 21.1.7.1.4. Signal strength (p. 501) | html | pdf |
- 21.1.7.1.5. Resolution (p. 501) | html | pdf |
- 21.1.7.1.6. Unit-cell parameters (p. 501) | html | pdf |
- 21.1.7.1.7. Symmetry (p. 501) | html | pdf |
- 21.1.7.2. Model quality, coordinates (pp. 501-504) | html | pdf |
- 21.1.7.2.1. Geometry and stereochemistry (pp. 501-502) | html | pdf |
- 21.1.7.2.2. Torsion angles (dihedrals) (pp. 502-503) | html | pdf |
- 21.1.7.2.3. Cα-only models (p. 503) | html | pdf |
- 21.1.7.2.4. Contacts and environments (p. 503) | html | pdf |
- 21.1.7.2.5. Noncrystallographic symmetry (p. 503) | html | pdf |
- 21.1.7.2.6. Solvent molecules (p. 503) | html | pdf |
- 21.1.7.2.7. Miscellaneous (pp. 503-504) | html | pdf |
- 21.1.7.3. Model quality, temperature factors (p. 504) | html | pdf |
- 21.1.7.4. Model versus experimental data (pp. 504-505) | html | pdf |
- 21.1.7.5. Accountancy (p. 505) | html | pdf |
- 21.1.7.1. Data quality (pp. 500-501) | html | pdf |
- 21.1.8. Future (p. 506) | html | pdf |
- References | html | pdf |