title: Preliminary crystallographic study of Thermus aquaticus glycerol kinase.
abstract: Glycerol kinase (GlpK) is an important enzyme which catalyzes the rate-limiting step in a central biochemical pathway involving glycerol metabolism. GlpK from the thermophile Thermus aquaticus has been overexpressed in glpK-deficient Escherichia coli and crystallized by the hanging-drop method. The crystal belongs to the cubic space group I23, with unit-cell parameters a = b = c = 163.94 (3) A. Native data were collected to 2.87 A resolution on a Cu Kalpha rotating-anode X-ray source.
authors: School of Pharmaceutical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Japan.
authors: H S
authors: HS
authors: Huang
authors: T
authors: T
authors: Inoue
authors: K
authors: K
authors: Ito
authors: T
authors: T
authors: Yoshimoto
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D005991:Glycerol Kinase / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D013824:Thermus / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D005991:Glycerol Kinase