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...

Popoln opis

Shranjeno v:
Bibliografske podrobnosti
izdano v:Acta Crystallogr F Struct Biol Commun
Main Authors: He, Miao, Zheng, Yingying, Huang, Chun-Hsiang, Qian, Guojun, Xiao, Xiansha, Ko, Tzu-Ping, Shao, Weilan, Guo, Rey-Ting
Format: Artigo
Jezik:Inglês
Izdano: International Union of Crystallography 2014
Teme:
Crystallization Communications
Online dostop: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
Oznake: Označite
Brez oznak, prvi označite!

Podobne knjige/članki