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Report No.

Crystallization and preliminary neutron diffraction studies of ADP-ribose pyrophosphatase-I from ${it Thermus thermophilus}$ HB8

Okazaki, Nobuo; Adachi, Motoyasu; Tamada, Taro; Kurihara, Kazuo; Oga, Takushi*; Kamiya, Nobuo*; Kuramitsu, Seiki*; Kuroki, Ryota

ADP-ribose pyrophosphatase-I from ${it Thermus thermophilus}$ HB8 (${it Tt}$ADPRase-I) prevents the intracellular accumulation of ADP-ribose by hydrolyzing it to AMP and ribose 5'-phosphate. To understand the catalytic mechanism of ${it Tt}$ADPRase-I, it is necessary to investigate the role of glutamates and metal ions as well as the coordination of water molecules located at the active site. A macroseeding method was developed in order to obtain a large ${it Tt}$ADPRase-I crystal which was suitable for a neutron diffraction study to provide structural information. Neutron and X-ray diffraction experiments were performed at room temperature using the same crystal. The crystal diffracted to 2.1 and 1.5 ${AA}$ resolution in the neutron and X-ray diffraction experiments, respectively. The crystal belonged to the primitive space group ${it P}$3$$_{2}$$21, with unit-cell parameters $$a$$ = $$b$$ = 50.7, $$c$$ = 119 ${AA}$.



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Category:Biochemical Research Methods



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