Crystallization of the N-terminal domain of the Escherichia coli regulatory protein TyrR

The N-terminal domain of the regulatory protein TyrR from Escherichia coli forms a dimer in solution and has been purified and crystallized. The crystals belong to space group C2 with unit-cell parameters a = 134.5, b = 72.1, c = 96.7 Å, β = 98.5°. The crystals diffract to 2.8 Å. Assuming a molecular weight of 23219 Da, a V_m of 2.5 ų Da⁻¹ is obtained for two dimers in the asymmetric unit.