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...
में बचाया:
| में प्रकाशित: | Proc Natl Acad Sci U S A |
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| मुख्य लेखकों: | , , , , |
| स्वरूप: | Artigo |
| भाषा: | Inglês |
| प्रकाशित: |
National Academy of Sciences
1995
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| विषय: | |
| ऑनलाइन पहुंच: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC40965/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7568114/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.92.20.9264 |
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