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![[Figure 1]](rr5137fig1mag.jpg)
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Figure 1
Structure of the U6 snRNP core with a wild-type ISL. (a) Sequences of the protein and RNA constructs used for crystallization. Regions colored white were deleted to promote crystallization. Gray regions in the Prp24 sequence correspond to linkers surrounding the RRM domains. U6 nucleotides 64–83 are disordered in one of the two complexes in the crystallographic asymmetric unit [gray complex in (b)]. (b) Packing interactions between the two complexes in the crystallographic asymmetric unit, which are related to each other by noncrystallographic twofold rotational symmetry. One U6–Prp24 complex is colored gray to enhance the contrast between the two complexes in the asymmetric unit. The electropositive groove is thought to bind double-stranded RNA to promote the formation of the U4/U6 di-snRNA (Montemayor et al., 2014  ; Didychuk et al., 2016). (c) Crystal-packing environment surrounding the asymmetric unit. Parallel cavities with cross-sections of approximately 1500 Å2 traverse the crystal lattice. (d) The two complexes in the asymmetric unit are virtually identical, with the exception of the U6 ISL, which in one complex is positioned in the center of the large solvent cavity and is disordered. |
![[Figure 1]](rr5137fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
