Figure 2.
Figure 2: Experimental electron density. a, F[Se] - F[native]
difference density (contoured at 4 )
in the EcClC P2[1]2[1]2[1] crystal form superimposed on an carbon
trace of the EcClC subunit viewed from outside the cell. Side
chains of methionine residues are shown in stick representation
with the position of the Se atom indicated by a green sphere.
The difference Fourier map was calculated to 4.0 Å and averaged
over the six subunits in the asymmetric unit. b, Electron
density map from the StClC P2[1] crystal form at 3.0 Å
resolution, contoured at 1 .
The map was calculated from native amplitudes and
solvent-flattened, averaged phases. The refined structure is
shown as a stick model. Figures 2 -6 were prepared with DINO
(http://www.dino3d.org).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2002,
415,
287-294)
copyright 2002.
)
in the EcClC P2[1]2[1]2[1] crystal form superimposed on an 
carbon
trace of the EcClC subunit viewed from outside the cell. Side
chains of methionine residues are shown in stick representation
with the position of the Se atom indicated by a green sphere.
The difference Fourier map was calculated to 4.0 Å and averaged
over the six subunits in the asymmetric unit. b, Electron
density map from the StClC P2[1] crystal form at 3.0 Å
resolution, contoured at 1