title: Crystallization and preliminary X-ray data for 3-isopropylmalate dehydrogenase of Thermus thermophilus.
abstract: The gene coding for 3-isopropylmalate dehydrogenase of Thermus thermophilus was cloned and expressed in Escherichia coli. The extracted enzyme was crystallized in a suitable size for X-ray crystallographic studies. The crystals have a space group of P3(1)21 or P3(2)21 with a = b = 78.6 A and c = 157.4 A.
authors.affiliation: Institute of Protein Research, Osaka University.
authors.forename: Y
authors.initials: Y
authors.lastname: Katsube
authors.forename: N
authors.initials: N
authors.lastname: Tanaka
authors.forename: A
authors.initials: A
authors.lastname: Takenaka
authors.forename: T
authors.initials: T
authors.lastname: Yamada
authors.forename: T
authors.initials: T
authors.lastname: Oshima
mesh_terms: D050539:3-Isopropylmalate Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000032:analysis*; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D011994:Recombinant Proteins; D013824:Thermus / Q000201:enzymology; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; D050539:3-Isopropylmalate Dehydrogenase