Overproduction, crystallization and preliminary diffraction data of ADP-ribose pyrophosphatase from Thermus thermophilus HB8

An ADP-ribose pyrophosphatase from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. Gel-filtration chromatography showed the protein to be in a dimeric state. This protein catalyses the Mg²⁺- or Zn²⁺-dependent hydrolysis of ADP-ribose to AMP and ribose-5′-phosphate. It was crystallized in the absence and the presence of ADP-ribose by the hanging-drop vapour-diffusion method. Complete data sets were collected to 1.50 Å resolution from the apo form using synchrotron radiation and to 2.0 Å resolution from the complexed form. Both crystals belong to space group P3₁21 or P3₂21 and contain one molecule in the asymmetric unit.