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

International Tables for Crystallography (2006). Vol. F. ch. 19.1, p. 421   | 1 | 2 |

Figure 19.1.5.1 

A. A. Kossiakoffa*

aDepartment of Biochemistry and Molecular Biology, CLSC 161A, University of Chicago, Chicago, IL 60637, USA
Correspondence e-mail: koss@cummings.uchicago.edu

[Figure 19.1.5.1]
Figure 19.1.5.1

Difference map of Asn34 in the trypsin structure. (a) In a protein X-ray analysis, the difference in scattering intensity between O and NH2 is much too small to be detected. In contrast, the neutron-scattering magnitudes of oxygen and nitrogen (5.8 f versus 9.4 f) are quite dissimilar, and there is additional scattering at the nitrogen site from the two bound deuterium atoms. The resulting differential is over 350%, quite large enough to be detected for well ordered side chains. The nitrogen and oxygen positions shown are from the X-ray model. The difference density indicates that the orientation of the nitrogen and oxygen atoms is incorrect and should be rotated by 180° around the Cβ–Cγ bond. (b) Difference map for Ser139. On well ordered hydroxyl side chains, the orientation of deuterium atoms can sometimes be assigned.