Towards structure analysis of ADP-ribose pyrophosphatase by neutron diffraction

Adachi, Motoyasu; Kuroki, Ryota; Kuramitsu, Seiki*; Oga, Takushi*

no journal, , 

ADPRase catalyzes the hydrolysis of ADP ribose to ribose 5' phosphate and AMP. The postulated role of ADPRase is to controll the cellular concentration of toxic nucleoside diphosphate devivatives. Although the crystal structure of ADPRase was solved by X-ray crystallography, it remains unclear the hydration mechanism involving hydrogen atoms by ADPRase. The objective is to reveal the detailed hydration mechanism of ADPRase using neutrron crystallogarpahy. In the symposium, we report preliminary diffraction experiment of ADPRase by neutron, preparation of large cystals in size and perdeuteration of ADPRase.