Assembly of the Complex between Archaeal RNase P Proteins RPP30 and Pop5

Figure 4

Chemical-shift-based secondary structure prediction of free RPP30 is consistent with its structural homology to Pho RPP30. Graph shows probability for each residue assigned to be either β sheet (blue above axis) or α helix (red below axis), as determined with the TALOS+ software [19]. Assigned secondary structure is given to each residue based on the highest probability for the residue to be either α Helix, β Sheet, or Loop. Loop residues are not indicated, while dots on the x-axis represent residues for which TALOS+ gave no prediction. For comparison, the secondary structure observed in crystals of the homologous Pho RPP30 is shown above the graph.