International Tables for Crystallography (2006). Vol. F. ch. 18.2, pp. 375-381
https://doi.org/10.1107/97809553602060000694 |
Chapter 18.2. Enhanced macromolecular refinement by simulated annealing
Contents
- 18.2. Enhanced macromolecular refinement by simulated annealing (pp. 375-381) | html | pdf | chapter contents |
- 18.2.1. Introduction (p. 375) | html | pdf |
- 18.2.2. Cross validation (p. 375) | html | pdf |
- 18.2.3. The target function (pp. 375-377) | html | pdf |
- 18.2.4. Searching conformational space (pp. 377-379) | html | pdf |
- 18.2.5. Examples (pp. 379-380) | html | pdf |
- 18.2.6. Multi-start refinement and structure-factor averaging (p. 380) | html | pdf |
- 18.2.7. Ensemble models (p. 380) | html | pdf |
- 18.2.8. Conclusions (p. 381) | html | pdf |
- References | html | pdf |
- Figures
- Fig. 18.2.2.1. Effect of resolution on coordinate-error estimates (p. 376) | html | pdf |
- Fig. 18.2.3.1. The Gaussian probability distribution forms the basis of maximum-likelihood targets in crystallographic refinement (p. 376) | html | pdf |
- Fig. 18.2.4.1. Illustration of simulated annealing for minimization of a one-dimensional function (p. 378) | html | pdf |
- Fig. 18.2.5.1. Simulated annealing produces better models than extensive conjugate-gradient minimization (p. 379) | html | pdf |
- Fig. 18.2.5.2. Maximum-likelihood targets significantly decrease model bias in simulated-annealing refinement (p. 380) | html | pdf |