Figure 26.1.3.9

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. 763 | 1 | 2 |

Figure 26.1.3.9

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 26.1.3.9

Photograph of sections z = 35/60 to 44/60 of the three-dimensional electron-density map of hen egg-white lysozyme at 2 Å resolution. AA′ shows the axis of a length of α-helix lying in the plane of the sections. B indicates an α-helix more nearly normal to the sections. C indicates the disulfide bridge between residues 30 and 115, the sulfur atoms of which lie one above the other. The side chain of a phenylalanine residue is located four residues along the helix from the disulfide, towards the lower sections. Reproduced with permission from Nature (Blake et al., 1965). Copyright (1965) Macmillan Magazines Limited.