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

ADP-ribose pyrophosphatase-I from Thermus thermophilus HB8 (TtADPRase-I) prevents the intracellular accumulation of ADP-ribose by hydrolyzing it to AMP and ribose 5′-phosphate. To understand the catalytic mechanism of TtADPRase-I, it is necessary to investigate the role of glutamates and metal ions ...

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Detaylı Bibliyografya
Asıl Yazarlar: Okazaki, Nobuo, Adachi, Motoyasu, Tamada, Taro, Kurihara, Kazuo, Ooga, Takushi, Kamiya, Nobuo, Kuramitsu, Seiki, Kuroki, Ryota
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: International Union of Crystallography 2011
Konular:
Crystallization Communications
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC3253833/
https://ncbi.nlm.nih.gov/pubmed/22232170
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309111044551
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