Figure 3.
Figure 3 Omit difference maps for the (A) NO- and (B) CO-bound
Axcyt c' structures contoured at 3.5 .
All the displayed atoms were omitted from the refinements (see
Materials and methods). However, Arg124 was retained in the
refinement, in order to remove distracting density, in
particular from the NO ligand. The view is chosen to emphasize
the flattening of the heme plane upon binding of CO. The atoms
are colored according to their temperature factors, which all
lie roughly in the range 10–40 Å^2, where dark blue
indicates a low value increasing through light blue, dark green,
light green, yellow and orange, to red, which indicates a high
value. Note that the side chain of His120 in the NO-bound
structure and the side chain of Leu16 and the propionate group A
in the CO-bound structure are less well defined in the electron
density and have relatively high thermal parameters. See main
text for a further explanation.
.
All the displayed atoms were omitted from the refinements (see
Materials and methods). However, Arg124 was retained in the
refinement, in order to remove distracting density, in
particular from the NO ligand. The view is chosen to emphasize
the flattening of the heme plane upon binding of CO. The atoms
are colored according to their temperature factors, which all
lie roughly in the range 10–40 Å^2, where dark blue
indicates a low value increasing through light blue, dark green,
light green, yellow and orange, to red, which indicates a high
value. Note that the side chain of His120 in the NO-bound
structure and the side chain of Leu16 and the propionate group A
in the CO-bound structure are less well defined in the electron
density and have relatively high thermal parameters. See main
text for a further explanation.