journal menu
![[Figure 5]](qo5004fig5mag.jpg)
|
|
Figure 5
Ribosomal protein L31e from the crystal structure of a large ribosomal subunit from H. marismortui. A solvent-exposed, poorly resolved loop following Phe X/77 was traced too short in the original model and resulted in a two-residue sequence-register shift in a C-terminal part of the chain. Strong difference-density peaks showing a few excess and missing atoms in the deposited structures for Ala X/83, Val X/85 and Ala X/87 (a) disappear after refining the model with the corrected sequence register (b). The combined 2mFo − DFc (blue) and difference mFo − DFc (red/green) maximum-likelihood maps calculated using REFMAC5 and PDB-REDO are shown at 1.5σ and 3σ levels, respectively. |
![[Figure 5]](qo5004fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
