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. Author manuscript; available in PMC: 2010 Oct 23.
Published in final edited form as: J Mol Biol. 2009 Aug 22;393(2):308–319. doi: 10.1016/j.jmb.2009.08.042

Figure 2.

Figure 2

Alternate conformations observed in the conserved loop region of human ferrochelatase consisting of residues 301–307 for monomer A (Panel a). The electron density for the same residues in monomer B (Panel b) was much cleaner and indicated a single conformation. In both panels the green cage represents a 2Fo-Fc composite omit map that was generated using the simulated annealing protocol with 7% of the model omitted per cycle and contoured at one sigma. Atom coloring is the same as that shown in Figure 1 except that the carbon atoms are colored yellow for the alternate conformations of residues 302, 303, and 304.