Figure 21.2.2.2

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. 510 | 1 | 2 |

Figure 21.2.2.2

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

Figure 21.2.2.2

Atomic volume Z score r.m.s. variation with nominal resolution (d spacing) in 900 protein structures from the PDB. (a) Average of the r.m.s. volume Z score computed for structures having the same resolution (to within $[\pm 0.1]$ Å). The vertical bars indicate the magnitude of the standard deviations of the r.m.s. volume Z score in individual d-spacing bins. Graph points are derived from less than 10 structures (open diamonds) and from more than 10 structures (filled diamonds). (b) R.m.s. Z-score values as in (a), displayed for individual structures as a function of resolution. The five furthest outlier proteins are marked by their PDB codes.