title: Cloning, expression, purification, crystallization and preliminary diffraction analysis of the C-terminal catalytic domain of human poly(ADP-ribose) polymerase.
abstract: Two fragments of the C-terminal catalytic domain of human poly(ADP-ribose) polymerase (catPARP), Met-catPARP and Gly-Ser-catPARP, were purified and crystallized. Both catPARP crystals belong to space group C2, with almost the same unit-cell parameters. However, the shapes and harvest periods of both crystals were quite different owing to the slight mutation at the N-terminal position. Gly-Ser-catPARP was found to be more suitable for X-ray crystallography and crystals showed diffraction to at least 3.5 A resolution.
authors.affiliation: Exploratory Research Laboratories, Fujisawa Pharmaceutical Co. Ltd, 5-2-3 Tokodai, Tsukuba, Ibaraki 300-2698, Japan. takayoshi_kinoshita@po.fujisawa.co.jp
authors.forename: Takayoshi
authors.initials: T
authors.lastname: Kinoshita
authors.forename: Takeshi
authors.initials: T
authors.lastname: Tsutsumi
authors.forename: Riyo
authors.initials: R
authors.lastname: Maruki
authors.forename: Masaichi
authors.initials: M
authors.lastname: Warizaya
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Ishii
authors.forename: Takashi
authors.initials: T
authors.lastname: Fujii
mesh_terms: D020134:Catalytic Domain; D003001:Cloning, Molecular; D003460:Crystallization; D006801:Humans; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D011065:Poly(ADP-ribose) Polymerases