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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Argitaratua izan da:	Proc Natl Acad Sci U S A
Egile Nagusiak:	Korolev, S, Nayal, M, Barnes, W M, Di Cera, E, Waksman, G
Formatua:	Artigo
Hizkuntza:	Inglês
Argitaratua:	National Academy of Sciences 1995
Gaiak:	Research Article
Sarrera elektronikoa:	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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