Global agreement between the model and experimental data

Wodak, S. J.; Vagin, A. A.; Richelle, J.; Das, U.; Pontius, J.; Berman, H. M.

doi:10.1107/97809553602060000708

International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

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International Tables for Crystallography (2006). Vol. F. ch. 21.2, p. 511 | 1 | 2 |

Section 21.2.3.1.1.2. Global agreement between the model and experimental data

S. J. Wodak,^a ^* A. A. Vagin,^b J. Richelle,^b U. Das,^b J. Pontius^b and H. M. Berman^c

^aUnité de Conformation de Macromolécules Biologiques, Université Libre de Bruxelles, avenue F. D. Roosevelt 50, CP160/16, B-1050 Bruxelles, Belgium, and EMBL–EBI, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, England, ^bUnité de Conformation de Macromolécules Biologiques, Université Libre de Bruxelles, avenue F. D. Roosevelt 50, CP160/16, B-1050 Bruxelles, Belgium, and ^cDepartment of Chemistry, Rutgers University, 610 Taylor Road, Piscataway, NJ 08854-8087, USA
Correspondence e-mail: shosh@ucmb.ulb.ac.be

21.2.3.1.1.2. Global agreement between the model and experimental data

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To evaluate the global agreement between the atomic model and the experimental data, the program computes three classical quality indicators: the R factor, $[R_{\rm free}]$ (Brünger, 1992b) and the correlation coefficient $[\hbox{CC}_{F}]$ between the calculated and observed structure-factor amplitudes (Table 21.2.3.1). The R factor is computed using all the reflections considered (except those approximated by their average value in the corresponding resolution shell) and applying the same resolution and σ cutoff as those reported by the authors. $[R_{\rm free}]$ is computed using the subset of reflections specified by the authors. In addition, the R factor is evaluated using the `non-free' subset of reflections (those not used to compute $[R_{\rm free}]$ ). The correlation coefficient is computed using all reflections from the reported high-resolution limit, applying the smooth low-resolution cutoff (see Table 21.2.3.1) but no σ cutoff.

References

Brünger, A. T. (1992b). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature (London), 355, 472–474.Google Scholar

International Tables for Crystallography (2006). Vol. F. ch. 21.2, p. 511