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Figure 3.
Figure 3. Structure of SnoaL2. (a) Structure of the SnoaL2
dimer. The secondary structure elements in subunit A are colored
differently, helices cyan and b-strands magenta. The part of
helix H5 in subunit A that is from the C-terminal linker/tag
peptide is shown in dark blue. The secondary structural elements
and the termini are labeled. Subunit B of the dimer is shown in
green. (b) Superposition of the two chains of SnoaL2. Chain A is
shown in cyan (the C-terminal linker/tag helix is colored dark
blue) and chain B in magenta. The orientation of the monomers is
the same as for chain A in (a). C[A] and C[B] indicate the C
termini of chain A and B, respectively. (c) Experimental MAD
electron density after solvent flattening and the final model
for the C termini of chain A and B, respectively. The chains are
colored as in (b) and the corresponding maps are shown in blue
for chain A and red for chain B. The maps are contoured at 1.5s.
The models and maps are superimposed according to the NCS.
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