Abstract
A putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3, an essential enzyme for polysaccharide biosynthesis, has been overexpressed in Escherichia coli and purified. Crystals were obtained using the oil-microbatch method at 291 K. A native data set extending to 1.8 A resolution has been collected and processed in space group P2(1). Assuming the presence of a dimer in the asymmetric unit, the V(M) value is calculated to be 2.3 A3 Da(-1), which is consistent with the result of a dynamic light-scattering experiment that shows a dimeric state of the protein in solution.