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The crystal structure of cyclic AMP–catabolite activator protein (CAP) fromEscherichia colicontaining cobalt(II) chloride and ammonium sulfate is reported at 1.97 Å resolution. Each of the two CAP subunits in the asymmetric unit binds one cobalt(II) ion, in each case coordinated by N-terminal domain residues His19, His21 and Glu96 plus an additional acidic residue contributedviaa crystal contact. The three identified N-terminal domain cobalt-binding residues are part of a region of CAP that isdoi:10.1107/s2053230x14005366 pmid:24817710 pmcid:PMC4014319 fatcat:3f6x6mc6q5dbhn2xoglefgf56a