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Figure 5
The quality of the electron-density maps reflects the good quality of the in situ data. (a) 2FoFc electron-density map after an OMIT map related to a C-terminal HiTehA deletion including TM10. The map is calculated at 2.3 Å resolution and contoured at 1.0σ. The fitted TM10 is shown for clarity. (b) Positive Fo − Fc electron-density map at 2.3 Å resolution contoured at 3.0σ showing the missing TM10. TM10 is also shown here for clarity. (c) The four-transmembrane-helix search model. The TM1–TM4 helices (yellow) superimpose well onto the TM7–TM10 helices (salmon). (d) 2FoFc electron-density map calculated using the molecular-replacement phases at 2.3 Å resolution contoured at 1.0σ. The missing part of the structure in the search model is revealed in the electron-density map and is well connected, with visible density for the side chains; the initial search model (yellow) and the built model (salmon red) are shown.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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