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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1; 63(Pt 5): 412–414.
Published online 2007 April 14. doi:  10.1107/S1744309107016685
PMCID: PMC2334993

Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-d-mannosamine dehydrogenase from Pyrococcus horikoshii OT3

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 Å resolution has been collected and processed in space group P21. Assuming the presence of a dimer in the asymmetric unit, the V M value is calculated to be 2.3 Å3 Da−1, which is consistent with the result of a dynamic light-scattering experiment that shows a dimeric state of the protein in solution.

Keywords: UDP-N-acetyl-d-mannosamine, polyscaccharide biosynthesis, Pyrococcus horikoshii OT3

Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of International Union of Crystallography