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Figure 3
Comparison of maps calculated from SAD and MAD phases using the same total amount of data (52.5°, space group I422). (a) SAD experimental map. (b) SAD map after density modification. (c) Two-wavelength MAD experimental map. (d) Two-wavelength MAD after density modification. The helical backbone of the protein (PDB code 1kq3 ) is displayed with the map. Note the areas of disconnected density near the solvent boundary between residues 359 and 362 in the SAD map after density modification (b). The density is somewhat better defined in this area in the experimental SAD map (a), which implies that in this case the SAD phases are not accurate enough to define the molecular envelope well. The MAD maps tend to show better continuity.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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