Figure 26.1.3.12

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

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International Tables for Crystallography (2006). Vol. F. ch. 26.1, p. 765 | 1 | 2 |

Figure 26.1.3.12

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 26.1.3.12

Stereo-photographs of a model of the lysozyme molecule to a scale of 2 cm to 1 Å. The main polypeptide chain is painted white, and nitrogen, oxygen and sulfur atoms are indicated by blue, red and green sleeving, respectively. Some hydrogen bonds are shown by red connections. Oxygen atoms of the acid side chains near the cleft, Glu 35, Asp 52, Asp 101 and Asp103, are shown by red hemispheres (Blake et al., 1967).