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Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability.
The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain is identical in fold to the equivalent region of the Klenow fragment of Escherichia coli DNA polymeras...
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| Huvudupphovsmän: | , , , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
1995
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC40965/ https://ncbi.nlm.nih.gov/pubmed/7568114 |
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