Cloning, expression, purification, crystallization and preliminary diffraction analysis of the C-terminal catalytic domain of human poly(ADP-ribose) polymerase.
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.
Kinoshita
Takayoshi
T
Exploratory Research Laboratories, Fujisawa Pharmaceutical Co. Ltd, 5-2-3 Tokodai, Tsukuba, Ibaraki 300-2698, Japan. takayoshi_kinoshita@po.fujisawa.co.jp
Tsutsumi
Takeshi
T
Maruki
Riyo
R
Warizaya
Masaichi
M
Ishii
Yoshinori
Y
Fujii
Takashi
T
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
D011994:Recombinant Proteins; D011065:Poly(ADP-ribose) Polymerases