Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2)

SCO6571 protein from Streptomyces coelicolor A3(2) was overexpressed and purified using Rhodococcus erythropolis as an expressing host. Crystals of selenomethionine-substituted SCO6571 have been obtained by vapor diffusion method. SCO6571 crystals diffract to 2.3 Å and were found to belong to the orthorhombic space group P212121 with unit cell parameters a = 84.5, b = 171.6, c = 184.8 Å. Six molecules in the asymmetric unit give a crystal volume per protein mass (VM) of 2.97 Å3 Da-1 and solvent content of 58.6 %. The structure was solved by the single wavelength anomalous diffraction (SAD) method. SCO6571 is a TIM-barrel fold protein that assembles into a hexameric molecule with D3 symmetry.