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Figure 3
(a) Detail of the electron-density map showing 2mFo − DFc (1.0σ) overlaid with mFo − DFc (2.5σ). The left-hand panels show close-ups centered on residues Leu12 and Trp34 of the human protein. The right-hand part shows that a better fit of electron density is reached when these residues are mutated into those present in chicken egg-white lysozyme, namely Met12 and Phe34. (b) Electron-density map (2mFo − DFc at 1σ overlaid with mFo − DFc at 2.5σ) of lysozyme at 2.1 Å resolution calculated from 40 233 single-crystal indexed diffraction patterns. The electron-density map covers the residues between 33 and 55.

IUCrJ
Volume 1| Part 4| May 2014| Pages 204-212
ISSN: 2052-2525
doi:10.1107/S2052252514010070