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Figure 11
Electron-density maps of the trypsin structure calculated at 3.5 Å (green), 3.0 Å (blue) and 2.8 Å (magenta) resolution and SAD phases from one Ca2+ and 14 S atoms contoured at 1σ. (a), (b) and (c) The electron density maps of β-sheet (Gln50–Ser54, Ser84–Val90 and Ile103–Lys109). Only main-chain atoms are displayed. (d), (e) and (f) The electron-density map covering residues Asp102–Lys107.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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