Quality control for modern bone collagen stable carbon and nitrogen isotope measurements

The following documents are included: Table S1. Amino acid compositions for collagen and non-collagenous proteins collected from published literature. All data are presented as residues/1000. Materials code: 1= bone, 2 = scale, 3=skin. Temperature code: 1 = cold water, 2 = warm water. Table S2. Statistical results: Shapiro Wilks tests for C:NAtomic for different taxonomic groups. Table S3. Results for Spearman’s ρ tests for collagen δ13C grouped by ascending C:NAtomic Table S4. Extent to which shifts C:NAtomic (resulting from lipid contamination) affect δ13C. Comparison made with data generated by recent studies (Guiry, et al. 2016; Szpak and Guiry In Prep) on the effects of collagen extractions methods on the elemental and isotopic compositions of 122 bones from 85 fish, mammal, and bird specimens from diverse taxa and environments. Four to five extraction procedures were applied to subsamples from each bone. Within each group of four to five samples per bone, the δ13C of the sample with the lowest C:NAtomic was subtracted from the δ13C of the other samples. Table shows mean difference in δ13C (Δ13C) for analyses binned into groups with ascending C:NAtomic. Spearman’s ρ tests identify the point at positive shifts in Δ13C corresponding with increasing C:NAtomic become significant. Statistically significant results in bold. Table S5. Mean amino acid compositions and corresponding C:NAtomic for vertebrate classes not shown in Table 3 ESM_References: A list of references to the data appearing in Table S1.