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 angstrom and were found to belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell parameters a = 84.5, b = 171.6, c = 184.8 angstrom. Six molecules in the asymmetric unit give a crystal volume per protein mass (V-M) of 2.97 angstrom(3) 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 D-3 symmetry.