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. 2022 Jul 27;8(30):eabo0517. doi: 10.1126/sciadv.abo0517

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Fig. 4. — (A) ITC binding curves and derived affinities (K_D) of APLF^AD wild-type (WT), the truncation mutant used for crystallization (APLF^AD-Δ = Δ), or the double (Y462A/F468A = DA-34; Y476A/W485A = DA-AB) and quadruple (Y462A/F468A/Y476A/W485A = QA) mutants titrated to octamer-mix. (B) Percentage of octamer-compatible and octamer-incompatible histone-histone lysine cross-links based on surface-accessible Cα-Cα distances in the nucleosomal structure (Protein Data Bank: 2PYO) identified by XL-MS.