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![[Figure 4]](rr5137fig4mag.jpg)
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Figure 4
An apparent intramolecular protein cross-link in RRM1. (a) Electron-density map spanning amino acids His63, Cys64 and Lys99 in RRM1 of Prp24. Similar density was visible for both protein molecules in the crystallographic asymmetric unit. (b) Annealed OMIT map for the same region as depicted in (a). The positions of all atoms in His63, Cys64 and Lys99 were fixed during a round of simulated annealing as implemented in PHENIX (Afonine et al., 2012  ) and then omitted from the calculation of the map shown here. The depicted interatomic distances are between the side-chain N atom of Lys99 and the S atom of Cys64 and between the side-chain N atom of Lys99 and the NE2 ring N atom of His63. (c) The cross-link changes the orientation of His63 to be amenable for crystal-packing contacts with a neighboring ISL. (d) The same ISL–protein packing contacts are not possible in the absence of the cross-link, where His63 adopts a different conformation (Montemayor et al., 2014). (e) Mutation of residues in the apparent cross-link does not cause a discernible growth phenotype in yeast. |
![[Figure 4]](rr5137fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
