 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ih5010fig1mag.jpg)
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Figure 1
Architecture, diversity and reconstructions of amyloids. (a) Schematic representation of helical symmetry parameters: helical rise (Δz, orange) and helical twist (Δφ, tan) with central helical z axis (blue). The arrow indicates helix handedness. Amyloid z-stack model showing rise (orange) and crossover distance (blue). (b) Cross-β-peptide arrangements of amyloid polymorphs grouped by amyloid protein. Single-chain polymorphs are shown in blue and double-chain polymorphs in orange/blue. AL59 and FOR010 represent patient identifiers from light-chain amyloidosis cases. (c) Contributors to amyloid polymorphism organized by molecular weight (Mw), including post-translational modifications (PTMs). (d) Cumulative EMDB depositions categorized by processing software: RELION (orange) and cryoSPARC (blue). Data for 2026 were omitted for annual comparison consistency. Helical reconstructions are highlighted in the inset. (e) Validation metrics for deposited amyloid reconstructions using Amyloid Atlas data. Q-scores and resolutions at FSC 0.143 for ex vivo and all annotated amyloid entries displayed as nested pie charts. |
![[Figure 1]](ih5010fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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