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. 2024 Sep 11;633(8030):662–669. doi: 10.1038/s41586-024-07935-7

Fig. 2. Characterizing single amino acid substitutions and ClpX stepping in PASTORs.

Fig. 2

a, PASTOR sequence composition. b, Filtered nanopore current trace of PASTOR–HDKER. Colour boundaries are defined by automated YY segmentation. c, Top, an example PASTOR trace. The red boxes show the manually segmented YY dips. Bottom, the black horizontal lines denote the mean of individual steps. d, Distribution of the mean number of residues per step in each of the YY dips; n = 776 YY dips. e, Step dwell-time distribution. f, Average signal trace for the transformed VRs of each amino acid after Euclidian alignment of all the VRs equidistantly stretched to the same length. The VRs of a charged amino acid are shown as a dashed line (n of VRs and experiments are shown in Extended Data Table 1).