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| Title | Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A. |
|---|---|
| Journal, issue, pages | J Mol Biol, Vol. 195, Issue 3, Page 555-579, Year 1987 |
| Publish date | Jun 5, 1987 |
Authors | M Leijonmarck / A Liljas / ![]() |
| PubMed Abstract | The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at ...The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors. |
External links | J Mol Biol / PubMed:3309338 |
| Methods | X-ray diffraction |
| Resolution | 1.7 Å |
| Structure data | ![]() PDB-1ctf: |
| Chemicals | ![]() ChemComp-SO4: ![]() ChemComp-HOH: |
| Source |
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Keywords | RIBOSOMAL PROTEIN |
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