Figure 4.
Figure 4 2F[obs] - 1F[calc] electron-density maps for (a) PfENR
and (b) TgENR contoured at 0.8 produced
after initial rigid-body refinement in REFMAC5 (Murshudov et
al., 1997[Murshudov, G., Vagin, A. & Dodson, E. (1997). Acta
Cryst. D53, 240-255.]). Both NAD^+ and triclosan were omitted
from the model during refinement, but are represented in stick
format in order to show their unambiguous position in the
initial electron-density maps. (c) Stereo diagram of the
residues responsible for forming a hydrogen-bonding network to
the NAD^+ cofactor in subunit A of TgENR. (d) Stereo diagram of
the triclosan-binding site of subunit A of TgENR, with the
active-site residues Tyr179, Tyr189, Lys197 and Phe243 labelled.
(c) and (d) use the colour scheme yellow, red, blue, green and
orange for carbon, oxygen, nitrogen, chlorine and phosphorus,
respectively, and were produced in TURBO-FRODO (Roussel et al.,
1990[Roussel, A., Fontecilla-Camps, J. C. & Cambillau, C.
(1990). Acta Cryst. A46, C66-C67.]).
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
328-338)
copyright 2007.
produced
after initial rigid-body refinement in REFMAC5 (Murshudov et
al., 1997[Murshudov, G., Vagin, A. & Dodson, E. (1997). Acta
Cryst. D53, 240-255.]). Both NAD^+ and triclosan were omitted
from the model during refinement, but are represented in stick
format in order to show their unambiguous position in the
initial electron-density maps. (c) Stereo diagram of the
residues responsible for forming a hydrogen-bonding network to
the NAD^+ cofactor in subunit A of TgENR. (d) Stereo diagram of
the triclosan-binding site of subunit A of TgENR, with the
active-site residues Tyr179, Tyr189, Lys197 and Phe243 labelled.
(c) and (d) use the colour scheme yellow, red, blue, green and
orange for carbon, oxygen, nitrogen, chlorine and phosphorus,
respectively, and were produced in TURBO-FRODO (Roussel et al.,
1990[Roussel, A., Fontecilla-Camps, J. C. & Cambillau, C.
(1990). Acta Cryst. A46, C66-C67.]).