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Figure 5.
FIGURE 5. Phasing and structures of BhCBM25 and BhCBM26. A,
anomalous difference peaks (red) and representative electron
density (blue; 0.39 electrons/Å3) contoured around the
iodotyrosine heavy atom sites used for SAD phasing of BhCBM25.
B, anomalous difference peaks (red) and representative electron
density (blue; 0.37 electrons/Å3) contoured around the
cadmium sites used for SAD phasing of BhCBM26. C, the overall
secondary structure of BhCBM25 as representative of the fold and
topology of both BhCBM25 and BhCBM26. Selected amino acid side
chains are shown in a "licorice" representation. Electron
density maps are maximum likelihood (29)/  [A] (44) weighted 2F[o]
- F[c] electron density maps.
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