P. Dunten et al., CRYSTALLIZATION OF 5-KETO-4-DEOXYURONATE ISOMERASE FROM ESCHERICHIA-COLI, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 678-680
Citations number
14
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
5-keto-4-deoxyuronate isomerase from Escherichia coli has been crystal
lized after partial purification. The isomerase was found to be enrich
ed in preparations of an unrelated recombinant protein. Crystals of th
e isomerase were obtained from two different precipitants despite the
fact that the recombinant protein represented roughly 90% of the total
protein present. The crystals diffract to 2.7 Angstrom resolution and
are suitable for a structure determination. The role of the isomerase
in E. coil is uncertain, as E. coil is not known to degrade the polys
accharides which are potential sources of 5-keto-4-deoxyuronate.