Crystallization and preliminary X-ray diffraction analysis of the S-adenosylhomocysteine hydrolase (SAHH) from Thermotoga maritima

S-Adenosylhomocysteine hydrolase (SAHH) catalyzes the reversible conversion of S-adenosylhomocysteine into adenosine and homocysteine. The SAHH from Thermotoga maritima (TmSAHH) was expressed in Escherichia coli and the recombinant protein was purified and crystallized. TmSAHH crystals belonging to...

पूर्ण विवरण

में बचाया:
ग्रंथसूची विवरण
में प्रकाशित:Acta Crystallogr F Struct Biol Commun
मुख्य लेखकों: He, Miao, Zheng, Yingying, Huang, Chun-Hsiang, Qian, Guojun, Xiao, Xiansha, Ko, Tzu-Ping, Shao, Weilan, Guo, Rey-Ting
स्वरूप: Artigo
भाषा:Inglês
प्रकाशित: International Union of Crystallography 2014
विषय:
Crystallization Communications
ऑनलाइन पहुंच:https://ncbi.nlm.nih.gov/pmc/articles/PMC4231867/
https://ncbi.nlm.nih.gov/pubmed/25372832
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X14013478
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