| Literature DB >> 3309338 |
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 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.Entities:
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Year: 1987 PMID: 3309338 DOI: 10.1016/0022-2836(87)90183-5
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469