Expression, crystallization and preliminary X-ray crystallographic analysis of cellobiose 2-epimerase from Dictyoglomus turgidum DSM 6724

Cellobiose 2-epimerase epimerizes and isomerizes β-1,4- and α-1,4-gluco-oligosaccharides. N-Acyl-D-glucosamine 2-epimerase (DT_epimerase) from Dictyoglomus turgidum has an unusually high catalytic activity towards its substrate cellobiose. DT_epimerase was expressed, purified and crystallized. Crystals were obtained of both His-tagged DT_epimerase and untagged DT_epimerase. The crystals of His-tagged DT_epimerase diffracted to 2.6 Å resolution and belonged to the monoclinic space group P2₁, with unit-cell parameters a = 63.9, b = 85.1, c = 79.8 Å, β = 110.8°. With a Matthews coefficient V_M of 2.18 ų Da⁻¹, two protomers were expected to be present in the asymmetric unit with a solvent content of 43.74%. The crystals of untagged DT_epimerase diffracted to 1.85 Å resolution and belonged to the ortho­rhombic space group P2₁2₁2₁, with unit-cell parameters a = 55.9, b = 80.0, c = 93.7 Å. One protomer in the asymmetric unit was expected, with a corresponding V_M of 2.26 ų Da⁻¹ and a solvent content of 45.6%.