title: Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis.
abstract: The enzyme 6-phospho-3-hexulose isomerase (YckF) from Bacillus subtilis has been prepared and crystallized in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop method at 291 K using polyethylene glycol 2000 monomethylether as precipitant. They diffract beyond 1.7 A using an in-house Cu Kalpha source and belong to either space group P6(5)22 or P6(1)22, with unit-cell parameters a = b = 72.4, c = 241.2 A, and have two molecules of YckF in the asymmetric unit.
authors.affiliation: School of Sciences, University of Sunderland, Sunderland SR1 3SD, England.
authors.forename: E J
authors.initials: EJ
authors.lastname: Taylor
authors.forename: S J
authors.initials: SJ
authors.lastname: Charnock
authors.forename: J
authors.initials: J
authors.lastname: Colby
authors.forename: G J
authors.initials: GJ
authors.lastname: Davies
authors.forename: G W
authors.initials: GW
authors.lastname: Black
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D019747:Aldose-Ketose Isomerases; C023918:phospho-3-hexuloisomerase