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-Structure paper
Title | NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus. |
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Journal, issue, pages | Eur. Biophys. J., Vol. 49, Page 223-230, Year 2020 |
Publish date | Apr 27, 2019 (structure data deposition date) |
Authors | Golubev, A. / Fatkhullin, B. / Gabdulkhakov, A. / Bikmullin, A. / Nurullina, L. / Garaeva, N. / Islamov, D. / Klochkova, E. / Klochkov, V. / Aganov, A. ...Golubev, A. / Fatkhullin, B. / Gabdulkhakov, A. / Bikmullin, A. / Nurullina, L. / Garaeva, N. / Islamov, D. / Klochkova, E. / Klochkov, V. / Aganov, A. / Khusainov, I. / Validov, S. / Yusupova, G. / Yusupov, M. / Usachev, K. |
External links | Eur. Biophys. J. / PubMed:32152681 |
Methods | X-ray diffraction / NMR (solution) |
Resolution | 1.48 Å |
Structure data | PDB-6rji: PDB-6rk3: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | TRANSLATION / Elongation factor P / EFP / EF-P / STRUCTURAL PROTEIN / Staphylococcus aureus / Ribosome |