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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...
Shranjeno v:
| izdano v: | Acta Crystallogr F Struct Biol Commun |
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| Main Authors: | , , , , , , , |
| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
International Union of Crystallography
2014
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| Teme: | |
| 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 |
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