title: Crystallization and preliminary X-ray crystallographic studies of phosphoenolpyruvate carboxykinase from Corynebacterium glutamicum.
abstract: Phosphoenolpyruvate carboxykinase (PCK) is a key enzyme involved in the regulation of gluconeogenesis. PCKs from higher animals require guanosine nucleotide for activity. PCK from Corynebacterium glutamicum is also GTP specific. X-ray diffraction data from a C. glutamicum PCK crystal were collected to 2.8 A resolution. The crystals were monoclinic, belonging to space group P2(1), with unit-cell parameters a = 71.7, b = 117.4, c = 161.3 A, beta = 92.9 degrees. The presence of two molecules in the crystallographic asymmetric unit gives a V(M) of 2.5 A(3) Da(-1) and a solvent content of 50.3%.
authors.affiliation: Department of Biochemistry, University of Saskatchewan, 107 Wiggins Road, Saskatoon, Saskatchewan S7N 5E5, Canada.
authors.forename: Sanjukta
authors.initials: S
authors.lastname: Aich
authors.forename: Fumie
authors.initials: F
authors.lastname: Imabayashi
authors.forename: Louis T J
authors.initials: LT
authors.lastname: Delbaere
mesh_terms: D000192:Actinomycetales / Q000201:enzymology*; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D006863:Hydrogen-Ion Concentration; D010729:Phosphoenolpyruvate Carboxykinase (GTP) / Q000737:chemistry*
chemical_list: D010729:Phosphoenolpyruvate Carboxykinase (GTP)