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. Author manuscript; available in PMC: 2007 Jun 21.

Published in final edited form as: J Mol Biol. 2006 Nov 11;366(1):165–178. doi: 10.1016/j.jmb.2006.11.031

Electron density for minMobA protein. These stereo pictures display several active site residues with (a) a 3.0 Å MAD-phased F_o electron density map and (b) a 2.1 Å SIGMAA⁵⁸-weighted 2F_o–F_c electron density map; these maps are contoured at 0.8 σ. The active site Mn atom is shown, bound by three histidine residues, along with the catalytic Tyr 25 and other nearby residues.

Electron density for minMobA protein. These stereo pictures display several active site residues with (a) a 3.0 Å MAD-phased F_o electron density map and (b) a 2.1 Å SIGMAA⁵⁸-weighted 2F_o–F_c electron density map; these maps are contoured at 0.8 σ. The active site Mn atom is shown, bound by three histidine residues, along with the catalytic Tyr 25 and other nearby residues.