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

Journal Article · · Acta Crystallographica. Section F
; ; ;  [1]
  1. Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148 (Japan)
A putative UDP-N-acetyl-d-mannosamine dehydrogenase from P. horikoshii OT3 has been crystallized in space group P2{sub 1}, with unit-cell parameters a = 80.28, b = 69.24, c = 83.10 Å, β = 114.4°. X-ray diffraction data have been collected to 1.80 Å resolution. 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 P2{sub 1}. Assuming the presence of a dimer in the asymmetric unit, the V{sub M} value is calculated to be 2.3 Å{sup 3} Da{sup −1}, which is consistent with the result of a dynamic light-scattering experiment that shows a dimeric state of the protein in solution.
OSTI ID:
22360318
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English