Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate.
X-ray diffraction studies to nominal resolutions of 3.0 A for unliganded aspartate carbamolytransferase (EC 2.1.3.2)(R32 crystal symmetry) and of 2.8 A for the complex of aspartate carbamoyltransferase with cytidine triphosphate (P321 crystal symmetry) have yielded traces of the polypeptide chains o...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1978
|
| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC392945/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/364472/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.75.11.5276 |
| Tagy: |
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
