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Figure 1
Tm0423 maps calculated from SAD and MAD phases using the same total amount of data (52.5°). (a) SAD experimental map. (b) SAD map after density modification. (c) Two-wavelength MAD experimental map. (d) Two-wavelength MAD after density modification. The part of the structure shown is an α-helix near the surface of the protein (the helix backbone is displayed). The arrows near the top of the view labeled A and B point to zones where the density-modified SAD map (b) has breaks in the electron density. The experimental SAD map (a) shows density for the A zone, but this density disappears after density modification. The two-wavelength MAD maps (c) and (d) exhibit continuous density over these areas.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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