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Crystallization and preliminary X-ray diffraction analysis of cyclolavandulyl diphosphate synthase, a new member of the cis-isoprenyl diphosphate synthase superfamily
Cyclolavandulyl diphosphate synthase (CLDS; estimated molecular weight 23.1 kDa) from the soil bacterium Streptomyces sp. CL190 is an enzyme that catalyzes both the condensation of two molecules of C(5) dimethylallyl diphosphate (DMAPP) and the subsequent cyclization. CLDS was crystallized in the ab...
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| Hlavní autoři: | , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
International Union of Crystallography
2014
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4188091/ https://ncbi.nlm.nih.gov/pubmed/25286951 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X14018883 |
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