Crystallization and preliminary X‐ray crystallographic analysis of human phosphodiesterase 12

Phosphodiesterase PDE12 is a medically important esterase‐family member that hydrolyzes 2′–5′‐linked oligoadenylates (2‐5A), which are involved in the regulation of biological processes related to the antiviral and antitumour activity that can be induced by interferons. Here, cloning, purification and crystallization of the C‐terminal endonuclease/exonuclease/phosphatase‐homology domain of human PDE12 is reported. The crystals belonged to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 111.3, c = 192.4 Å, and diffracted to 2.5 Å resolution. Assuming the presence of three molecules in the asymmetric unit, the solvent content was estimated to be about 44.0%.