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-Structure paper
Title | Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold. |
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Journal, issue, pages | J. Biomol. Struct. Dyn., Vol. 36, Page 4392-4404, Year 2018 |
Publish date | Jul 13, 2017 (structure data deposition date) |
Authors | Timofeev, V.I. / Altukhov, D.A. / Talyzina, A.A. / Agapova, Y.K. / Vlaskina, A.V. / Korzhenevskiy, D.A. / Kleymenov, S.Y. / Bocharov, E.V. / Rakitina, T.V. |
External links | J. Biomol. Struct. Dyn. / PubMed:29283021 |
Methods | NMR (solution) / X-ray diffraction |
Resolution | 2.25 Å |
Structure data | PDB-5ogu: PDB-7pzo: |
Chemicals | ChemComp-SO4: ChemComp-HOH: |
Source |
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Keywords | DNA BINDING PROTEIN / ALLERGEN |