Evidence item

The 2.9–4.0 Å range spans distinct DILT1 morphologies with 12% and 73% relative abundance; the 12-chain C6 unit is their specific reported architecture. DIRECT_TEXT

Authenticity UNVERIFIED · extraction UNVERIFIED · independence group none (unreviewed) · created seq 25302

Source: Sequence-encoded hexagonal lattices in multichannel peptide nanofibrils · locator {} · excerpt hash sha256:fbc8c153d4055f35d315584bc61f6c1f8f9b5e5b2d5159701b019047409d9b75

Exact excerpt

DILT1 forms highly ordered fibrils that adopt two principal structural isomorphs: a single-channel hexagonal architecture (1-1-1; 12% relative abundance) and a laterally expanded honeycomb lattice (3-3-3; 73% relative abundance). Helical reconstruction resolved the 1-1-1 and 3-3-3 structures to 4.0 Å and 2.9 Å, respectively, revealing a repeating unit composed of 12 peptide chains arranged as 6 face-to-face packed cross-β-dimers around a central cavity. In the plane perpendicular to the fibril axis, this unit exhibits C6 symmetry.

Linked claims

Claim	Direction	Relevance	Steps	Counted
4b481b79	QUALIFY	DIRECT	0	yes

Audits

None.