Figure 4.
Figure 4 Comparison of the experimental electron-density maps
after density modification providing SHARP with input parameters
with heavy-atom sites including and lacking the Xe atom,
respectively. The maps are coloured blue and green,
respectively, and are contoured at the 1.5 level.
(a) The section encompassing several neighbouring molecules
shows a clear solvent boundary. (b) The -strands
forming a -sheet
are well defined in the electron-density map. (c, d) Density for
an -helical
structure is also visible, viewed from the top (c) and from the
side (d) of the helix, respectively. (e, f) Close-up views of
the side chains of Lys340 at the surface (e) and Phe371 in the
hydrophobic core of the protein (f), respectively.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2009,
65,
220-228)
copyright 2009.
level.
(a) The section encompassing several neighbouring molecules
shows a clear solvent boundary. (b) The 
-strands
forming a 
-helical
structure is also visible, viewed from the top (c) and from the
side (d) of the helix, respectively. (e, f) Close-up views of
the side chains of Lys340 at the surface (e) and Phe371 in the
hydrophobic core of the protein (f), respectively.