Extended Data Fig. 3: Euclidian distances for crosslinks observed between modelled residues (Cα) of the 17S U2 snRNP.
a–c, Crosslinks from a single 17S U2 crosslinking experiment (with two technical replicates) were identified by pLink2.3.5 and filtered to a false discovery rate (FDR) of 1% (a), pLink1.23 at an FDR of 1% (b), and pLink1.23 at an FDR of 5% (c). Calculations were performed using PyMOL2.3.4 for crosslinks with a score of at least 1. Most crosslinks (93–95% at the spectral level and 85–86% at the unique crosslink level) are consistent—that is, Cα atoms of the crosslinked amino acids are within 30 Å of each other—in the presented model of the 17S U2 snRNP. The percentage of overlength crosslinks (that is, longer than 30 Å) is slightly higher than observed for more rigid complexes, which is consistent with the known structural flexibility/dynamics of the 17S U2 snRNP.
