Figure 2.
Fig. 2. (A) Comparison of experimental and final maps. An
area around the active site residue Glu144 is drawn in a stick
representation. A 1 contoured
F[o], MLPHARE map
is shown in black, calculated by using the phases at the end of
heavy atom refinement with MLPHARE. A 2F[o]-F[c], [calc] map is
shown at the end of refinement with CNS, contoured at 1.4 (in red).
(B) The two molecules in the asymmetric unit, color-coded to
identify various regions. The TIM barrel (gray), the / -domain
(yellow), the support loop (red), the linker (blue), and the
ChBD (green). (C) ChiB, as in Fig. 2B, with the flexible loop
covering the active site (green), the active site residue (red
sticks), the porch loop (orange), and the exposed aromatic
residues (black sticks). (D) Superposition of the ChBD of ChiB
(blue ribbon) and the CeBD of endoglucanase Cel5 (gray ribbon).
Most of the support loop of the catalytic domain of ChiB is
shown as a dark-blue ribbon. Trp252 also is shown in magenta.
The substrate-binding residues for the CeBD are shown in yellow,
and the equivalent residues in the ChBD are shown in magenta.
The disulfide bond between the termini of the CeBD is shown in
green. Polar residues lining the path of aromatic residues in
ChiB are shown in magenta. Labels correspond to the ChiB
sequence. Note the almost exact overlap of the conserved -strands.
contoured
F[o], 
MLPHARE map
is shown in black, calculated by using the phases at the end of
heavy atom refinement with MLPHARE. A 2F[o]-F[c], 
/ 
-domain
(yellow), the support loop (red), the linker (blue), and the
ChBD (green). (C) ChiB, as in Fig. 2B, with the flexible loop
covering the active site (green), the active site residue (red
sticks), the porch loop (orange), and the exposed aromatic
residues (black sticks). (D) Superposition of the ChBD of ChiB
(blue ribbon) and the CeBD of endoglucanase Cel5 (gray ribbon).
Most of the support loop of the catalytic domain of ChiB is
shown as a dark-blue ribbon. Trp252 also is shown in magenta.
The substrate-binding residues for the CeBD are shown in yellow,
and the equivalent residues in the ChBD are shown in magenta.
The disulfide bond between the termini of the CeBD is shown in
green. Polar residues lining the path of aromatic residues in
ChiB are shown in magenta. Labels correspond to the ChiB
sequence. Note the almost exact overlap of the conserved