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...

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Détails bibliographiques
Publié dans:Acta Crystallogr F Struct Biol Commun
Auteurs principaux: He, Miao, Zheng, Yingying, Huang, Chun-Hsiang, Qian, Guojun, Xiao, Xiansha, Ko, Tzu-Ping, Shao, Weilan, Guo, Rey-Ting
Format: Artigo
Langue:Inglês
Publié: International Union of Crystallography 2014
Sujets:
Crystallization Communications
Accès en ligne: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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