Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus

Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 Å resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C222₁, with unit-cell parameters a = 171.0, b = 231.6, c = 124.9 Å. The crystal contains three molecules in an asymmetric unit (V_M = 2.11 Å³ Da^-1) and has a solvent content of 61.5%.