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. Author manuscript; available in PMC: 2008 Sep 2.
Published in final edited form as: Science. 2008 Jul 11;321(5886):250–253. doi: 10.1126/science.1157987

Figure 3.

Figure 3

(A) Anomalous difference Fourier map calculated at 5.2 Å resolution illustrating the binding of selenomethionine to the C2-domains of MetNI following a 1 mM soak of transporter crystals. The electron density is contoured at 6 times the standard deviation of the map. (B) Comparison of the relative orientations of C2-domains observed in the MetNI and free MetN-C2 structures, following superposition of one subunit in each dimer. The green and dark gray traces correspond to the C2-domain dimer in MetNI, while the magenta and light gray traces represent the isolated C2-domain structure. The binding site for selenomethionine is denoted by the gold surface. The view is roughly perpendicular about the horizontal axis from that in (A).