Crystallization and preliminary X‐ray studies of dUTPase from Mason–Pfizer monkey retrovirus

Deoxyuridine 5′‐triphosphate nucleotidohydrolase from Mason–Pfizer monkey retrovirus (M‐PMV dUTPase) is a betaretroviral member of the dUTPase enzyme family. In the mature M‐PMV virion, this enzyme is present as the C‐­terminal domain of the fusion protein nucleocapsid‐dUTPase. The homotrimeric organization characteristic of dUTPases is retained in this bifunctional fusion protein. The fusion protein supposedly plays a role in adequate localization of dUTPase activity in the vicinity of nucleic acids during reverse transcription and integration. Here, the nucleocapsid‐free dUTPase (48 426 Da) was cocrystallized with a dUTP substrate analogue using the hanging‐drop vapour‐diffusion method. The obtained crystals belong to the primitive hexagonal space group P 6 3 , with unit‐cell parameters a = 60.6, b = 60.6, c  = 63.6 Å, α = 90, β = 90, γ = 120°. Native and PtCl 4 ‐derivative data sets were collected using synchrotron radiation to 1.75 and 2.3 Å, respectively. Phasing was successfully performed by isomorphous replacement combined with anomalous scattering.