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1 M40 Signal leaved RS1 Domain Discoidin Domain β- β- M M e e O O H H His 6 -Tag * Supplementary Figure 1 Purification of wild-type retinoschisin. () Schematic diagram of the retinoschisin construct used for these studies, with residues required for disulphide formation marked. () SDS-PGE gel of retinoschisin after Ni-NT affinity purification, disulphide-dependent octamer formation indicated by *. () SE-MLS purification of retinoschisin, showing separation of Octamer, Dimer and Monomer species with molecular weights of ~200, 54 and 27kDa respectively.
2 R g =31.6Å Supplementary Figure 2 SXS analysis of wild-type retinoschisin monomer. () The rotationally averaged scatter profile of purified retinoschisin monomer (LogI(q) vs. q) with the GNOM fit superimposed to the scatter curve.() R g normalized kratky plot of the retinoschisin monomer ((I(q)/I(0))(qR g ) 2 vs. qr g ) showing a peak consistent with a folded protein. Shown are the cross-hairs for globularity of the protein fold (1.1 vs.. This analysis suggests a folded, elongated structure. () Guinier plot (LogI(q) vs. q 2 ) of the low q region, showing a Radius of Gyration (R g ) of 31.6Å for the retinoschisin monomer with plotted residuals for the guinier region.
3 D leaved α-factor Discoidin Domain His 6 - Signal Tag E F G R g =15.6Å Supplementary Figure 3 Purification of mammalian discoidin domain from Pichia pastoris. () Schematic diagram of the construct expressed and secreted by Pichia pastoris. () Western blot of the elute from Ni-NT chromatography probed with anti-his 6 antibody () oomassie blue stained SDS- PGE of size-exclusion chromatography elution. (D) 280 profile of the discoidin domain from the SE- SXS experiment. (E) The rotationally averaged scatter profile of the discoidin domain (LogI(q) vs. q) with the GNOM fit superimposed to the scatter curve. (F) R g normalized kratky plot of the discoidin domain ((I(q)/I(0))(qR g ) 2 vs. qr g ) showing a peak consistent with a folded protein. Shown are the crosshairs for globularity of the protein fold (1.1 vs.. (G) Guinier plot (LogI(q) vs. q 2 ) of the low q region, showing R g of 15.6Å for the discoidin domain with plotted residuals for the guinier region.
4 Supplementary Figure 4 ryo-electron microscopy of retinoschisin. () Representative cryo-em image with a field of dispersed particles for wild-type and () R141H octamers.
5 15.9Å 0 o 13.6Å 12.8Å D 180 o 0 o 9.3Å E F 50Å Supplementary Figure 5 Resolution estimation of the wild-type octamer and dimer of octamers maps. () Final Fourier shell correlation (FS) of the RELION-refined octamer map. Shown are resolution estimates at 0.5 and correlations. () Euler angle distribution of the octamer 3D reconstruction. () Final FS of the RELION-refined dimer of octamers map. Shown are resolution estimates at 0.5 and correlations. (D) Euler angle distribution of the dimer of octamers 3D reconstruction. (E) ResMap-H2 analysis of the dimer of octamers map, showing the relative proportions of voxels observed at different resolutions. (F) ResMap-H2 analysis visualised on wild-type dimer of octamers structure, showing local resolution variations throughout the map.
6 56.5 o 61.6 o D WT: 60.9 o R141H: 59.8 o E Supplementary Figure 6 omparative thermal stability of wild-type, R141H and H207Q retinoschisin. () arycentric Mean Intrinsic Fluorescence Measurements of wild-type and H207Q retinoschisin monomer across a temperature range of 20-, with the differentials of the temperature ramp shown in (), giving the T m for both species. () arycentric Mean Intrinsic Fluorescence Measurements of wild-type and R141H retinoschisin monomer across a temperature range of 20-, with the differentials of the temperature ramp shown in (D), giving similar T m for both species. (E) Static Light Scattering at 473nm for wild-type and R141H monomers across a temperature range of 20 showing similar onset of aggregation for both species.
7 0 o 50Å 6.0Å 4.2Å D E 50Å Supplementary Figure 7 Resolution estimation of the R141H dimer of octamers structure. () The application of the soft Gaussian mask to the retinoschisin dimer of octamers and the resulting masked structure used for domain fitting and resolution estimation is shown. () Final FS of the masked RELION-refined map. Shown are resolution estimates at 0.5 and correlations. () Euler angle distribution of the 3D reconstruction. (D) ResMap-H2 analysis of the R141H map, showing the relative proportions of voxels observed at different resolutions. (E) ResMap-H2 analysis visualised on R141H structure, showing local resolution variations throughout the map, regions with reduced resolution are marked with arrows.
8 β1 Sp1 Sp2 β2 β3 Sp3 β4 β5 β6 β7 β8 i N-terminal Region ii β8 β3 1 E72 S73 N104 2 L161 N162 W163 Y165 25Å β5 Loop between β4 and β5 T185 S184 3 N172 N173 β4 β7 Loop between β4 and β5 25Å β4 Supplementary Figure 8 Mapping of discoidin domain interfaces in the quasi-atomic model. () PDePIS analysis of the interfaces within the hexadecamer. Residues which contribute to the intra-octamer interface are shown in blue and residues involved in the inter-octamer interface highlighted in red. (i) The intra-octamer interface between subunits within the octamer is shown with residues identified by PDePIS highlighted. (ii) The intraoctamer interface contains 3 main contact points, with residues in these regions labelled. () The inter-octamer interface is shown with PDePIS-identified regions shown in red.
9 G70 D158 I195 R o K167 E215 I136 25Å 101 N104 E72, S73 P192, P193 T185 T138 R213 Outer Face Inner Face R209 H207 E146 D145 N179 G178 25Å Supplementary Figure 9 - Mapping XLRS-causative conservative mutations onto the quasi-atomic model. () The positions of non-cysteine, conservative XLRS-causative mutations which map to the intra-octamer interface are displayed in red. Shown are the mutations in the interface from both the outer and inner faces of the discoidin domain ring structure within the octamer. () Non-cysteine conservative XLRS-causative mutations, which map to the interoctamer interface, are highlighted in red.
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