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 Rmerge was 4.2% and the data completeness was 90.1%.