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Figure 2.
Fig. 2. (A) Initial electron density showing the overall
conformation of the duplicated sequence, as seen in space group
P3[2]21. The WT* structure, omitting residues 36-42 (shown as a
ribbon drawing) was subject to 10 cycles of rigid-body
refinement in the mutant lysozyme cell. The calculated phases
and structure factors, F[c], were used to calculate a map with
amplitudes (F[mutant]  F[c]) at
3.0-Å resolution. The density in the vicinity of the
deleted residues, contoured at 2.5  , is shown.
(B) Electron density after refinement of the inserted region in
space group P3[2]21. Coefficients are (2F[o]-F[c]). The
structure factors, F[c], and phases were calculated from the
refined model including the inserted region. The resolution is
2.5 Å, and the map is contoured at 1.0 . (C)
Superposition of the overall structure of the duplication mutant
in space group P3[2]21 (blue bonds) on WT* lysozyme (green
bonds). The inserted region in the mutant structure is
highlighted in yellow.
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