Figure 26.1.3.3

Blake, C. C. F.; Fenn, R. H.; Johnson, L. N.; Koenig, D. F.; Mair, G. A.; North, A. C. T.; Oldham, J. W. H.; Phillips, D. C.; Poljak, R. J.; Sarma, V. R.; Vernon, C. A.

doi:10.1107/97809553602060000725

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

pdf | chapter contents | chapter index | related articles

International Tables for Crystallography (2006). Vol. F. ch. 26.1, p. 758 | 1 | 2 |

Figure 26.1.3.3

C. C. F. Blake,^a ^‡ R. H. Fenn,^a ^§ L. N. Johnson,^a ^*^¶ D. F. Koenig,^a ^‡‡ G. A. Mair,^a ^‡‡ A. C. T. North,^a ^§§ J. W. H. Oldham,^a ^¶¶ D. C. Phillips,^a ^¶¶ R. J. Poljak,^a ^‡‡‡ V. R. Sarma^a ^§§§ and C. A. Vernon^b ^¶¶

^a Davy Faraday Research Laboratory, The Royal Institution, London W1X 4BS, England, and ^bDepartment of Chemistry, University College London, Gower Street, London WC1E 6BT, England
Correspondence e-mail: louise@biop.ox.ac.uk

Figure 26.1.3.3

Solid model of the electron density greater than about 0.5 e Å⁻³ in the second study of lysozyme at 6 Å resolution. This view of the model is equivalent to a view of the original model seen horizontally from the right of Fig. 26.1.2.13(c). (a) The new model has a marked cleft running roughly vertically down the other side of the model, corresponding to the one that can be seen in Fig. 26.1.2.13(c). (b) The cleft was shown to bind inhibitor molecules. The black density is that observed for the lysozyme–GlcNAc complex at 6 Å resolution.