International Tables for Crystallography (2006). Vol. F. ch. 16.1, pp. 333-345
https://doi.org/10.1107/97809553602060000689 |
Chapter 16.1. Ab initio phasing
Contents
- 16.1. Ab initio phasing (pp. 333-345) | html | pdf | chapter contents |
- 16.1.1. Introduction (p. 333) | html | pdf |
- 16.1.2. Normalized structure-factor magnitudes (pp. 333-334) | html | pdf |
- 16.1.3. Starting the phasing process (pp. 334-335) | html | pdf |
- 16.1.4. Reciprocal-space phase refinement or expansion (shaking) (pp. 335-336) | html | pdf |
- 16.1.5. Real-space constraints (baking) (p. 336) | html | pdf |
- 16.1.6. Fourier refinement (twice baking) (pp. 336-337) | html | pdf |
- 16.1.7. Computer programs for dual-space phasing (pp. 337-339) | html | pdf |
- 16.1.8. Applying dual-space programs successfully (pp. 339-344) | html | pdf |
- 16.1.8.1. Utilizing Pattersons for better starts (p. 340) | html | pdf |
- 16.1.8.2. Avoiding false minima (pp. 340-341) | html | pdf |
- 16.1.8.3. Data resolution and completeness (p. 341) | html | pdf |
- 16.1.8.4. Choosing a refinement strategy (pp. 342-343) | html | pdf |
- 16.1.8.5. Expansion to P1 (p. 343) | html | pdf |
- 16.1.8.6. Substructure applications (pp. 343-344) | html | pdf |
- 16.1.9. Extending the power of direct methods (pp. 344-345) | html | pdf |
- References | html | pdf |
- Figures
- Fig. 16.1.3.1. The conditional probability distribution of the three-phase structure invariants (p. 334) | html | pdf |
- Fig. 16.1.7.1. A flowchart for the Shake-and-Bake procedure, which is implemented in both SnB and SHELXD (p. 337) | html | pdf |
- Fig. 16.1.7.2. A histogram of figure-of-merit values (minimal function) for 378 scorpion toxin II trials (p. 338) | html | pdf |
- Fig. 16.1.7.3. Tracing the history of a solution and a nonsolution trial for scorpion toxin II as a function of Shake-and-Bake cycle (p. 338) | html | pdf |
- Fig. 16.1.8.1. Success rates for triclinic lysozyme are strongly influenced by the size of the parameter-shift angle (p. 341) | html | pdf |
- Fig. 16.1.8.2. (a) Mean phase error as a function of resolution for the two independent ab initio SHELXD solutions of the previously unsolved protein hirustasin (p. 341) | html | pdf |
- Fig. 16.1.8.3. (a) Success rates and (b) cost effectiveness for several dual-space strategies as applied to a 148-atom P1 structure (p. 342) | html | pdf |
- Fig. 16.1.8.4. Success rates for the 317-atom structure of gramicidin A (p. 343) | html | pdf |
- Tables
- Table 16.1.2.1. Theoretical values pertaining to 's (p. 334) | html | pdf |
- Table 16.1.7.1. Recommended parameter values for the SnB program (p. 338) | html | pdf |
- Table 16.1.8.1. Some large structures solved by the Shake-and-Bake method (p. 339) | html | pdf |
- Table 16.1.8.2. Overall success rates for full structure solution for hirustasin using different two-atom search vectors chosen from the Patterson peak list (p. 340) | html | pdf |
- Table 16.1.8.3. Success rates for three P1 structures illustrate the importance of using complete data to the highest possible resolution (p. 342) | html | pdf |
- Table 16.1.8.4. Improving success rates by `completing' the vancomycin data (p. 342) | html | pdf |