Crystallization and preliminary X-ray analysis of L-­serine 3-dehydrogenase complexed with NADP⁺ from the hyperthermophilic archaeon Pyrobaculum calidifontis

An NAD(P)⁺-dependent L-serine 3-dehydrogenase from the hyperthermophilic archaeon Pyrobaculum calidifontis was crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 120.81, b = 57.40, c = 56.37 Å, β = 106.88°. Diffraction data were collected to 1.57 Å resolution on beamline NE3A at the Photon Factory. The overall R_merge was 4.2% and the data completeness was 90.1%.