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

好熱菌${it Thermus thermophilus}$ HB8由来ADPリボースピロホスファターゼIの結晶化及び中性子回折研究

岡崎 伸生; 安達 基泰; 玉田 太郎; 栗原 和男; 大賀 拓史*; 神谷 信夫*; 倉光 成紀*; 黒木 良太

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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パーセンタイル:20.29

分野:Biochemical Research Methods

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