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. Author manuscript; available in PMC: 2009 Feb 15.
Published in final edited form as: J Mol Biol. 2007 Dec 4;376(2):317–324. doi: 10.1016/j.jmb.2007.11.084

Figure 2.

Figure 2

Close view of the structure around residue Glu255. (a) 2Fo-Fc electron density map contoured at 1.8 σ around (Chain B). Note that a molecule of glycerol occupies the space that is typically engaged by the side chain of Lys255. (b) Superimposition of Chains A (gray Cα atoms) and B (yellow Cα atoms). Note that chain A also contains a molecule of glycerol in the space near the mutation, but its location is somewhat different from that of Chain B.