taxonID	type	format	identifier	references	title	description	created	creator	contributor	publisher	audience	source	license	rightsHolder	datasetID
03E6B675FFA2345D01CB95E1FA41FD36.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/3748975/files/figure.png	https://doi.org/10.5281/zenodo.3748975	Figure 1. Amide I sub-band localisation of untreated and treated chicken type I collagen in SR-FTIR spectra.Sub-bands (β-sheet, ~1633cm−1; triple-helix, ~1658–1660cm−1; intermolecular, ~1683–1690cm−1) are indicated in the figures. Red traces denote second derivatives of experimental curves. Although the intermolecular sub-band typically presents at lower wavenumber, the identified value was the nearest local minimum in each of the second derivative traces and consistently appears across all samples; therefore, in this sample, the intermolecular sub-band was indexed at 1697–1699cm−1.	Figure 1. Amide I sub-band localisation of untreated and treated chicken type I collagen in SR-FTIR spectra.Sub-bands (β-sheet, ~1633cm−1; triple-helix, ~1658–1660cm−1; intermolecular, ~1683–1690cm−1) are indicated in the figures. Red traces denote second derivatives of experimental curves. Although the intermolecular sub-band typically presents at lower wavenumber, the identified value was the nearest local minimum in each of the second derivative traces and consistently appears across all samples; therefore, in this sample, the intermolecular sub-band was indexed at 1697–1699cm−1.	2019-10-30	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer		Zenodo	biologists	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer			
03E6B675FFA2345D01CB95E1FA41FD36.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/3748977/files/figure.png	https://doi.org/10.5281/zenodo.3748977	Figure 2. Microscopy images of T.rex vascular tissue and associated analysis of fibrillar collagen banding. (a) Transmitted VLM of T.rex soft tissue shows an extensive network of hollow, pliable, vascular structure and typical brown hue. (b) SEM image of the surface of a vessel.(c) Magnified image of (b) detailing features consistent with collagen fibre bundles (collagen fibril, “f”; collagen fibre, “CF”). Average fibril width was measured as 110nm, and average fibre width, 1.0µm. (d) TEM image of fibrous features observed in a longitudinal vessel cross-section. Intensity profiles of banded texture in (e) boxes 1 and 2 in c and (f) boxes 3, 4, 5 in (d) with example peak-to-peak distances (SEM average, ~74nm; TEM, ~56nm) called out in red. See Fig. S6 for precise d-spacing values determined using SAXS. For comparison to a modern blood vessel network in bone, see Fig. 5b of ref.39.	Figure 2. Microscopy images of T.rex vascular tissue and associated analysis of fibrillar collagen banding. (a) Transmitted VLM of T.rex soft tissue shows an extensive network of hollow, pliable, vascular structure and typical brown hue. (b) SEM image of the surface of a vessel.(c) Magnified image of (b) detailing features consistent with collagen fibre bundles (collagen fibril, “f”; collagen fibre, “CF”). Average fibril width was measured as 110nm, and average fibre width, 1.0µm. (d) TEM image of fibrous features observed in a longitudinal vessel cross-section. Intensity profiles of banded texture in (e) boxes 1 and 2 in c and (f) boxes 3, 4, 5 in (d) with example peak-to-peak distances (SEM average, ~74nm; TEM, ~56nm) called out in red. See Fig. S6 for precise d-spacing values determined using SAXS. For comparison to a modern blood vessel network in bone, see Fig. 5b of ref.39.	2019-10-30	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer		Zenodo	biologists	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer			
03E6B675FFA2345D01CB95E1FA41FD36.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/3748979/files/figure.png	https://doi.org/10.5281/zenodo.3748979	Figure 3. SR-FTIR full spectra of isolated T. rex vascular tissue and chicken type I collagen (no treatment). All key bands for the identification of protein (Amide I, Amide II, Amide III) are present in the dinosaur tissue spectrum. The T. rex spectrum also presents a strong non-peptide carbonyl (C=O) band at 1739cm−1 and a carbohydrate band at ~1010 cm−1.	Figure 3. SR-FTIR full spectra of isolated T. rex vascular tissue and chicken type I collagen (no treatment). All key bands for the identification of protein (Amide I, Amide II, Amide III) are present in the dinosaur tissue spectrum. The T. rex spectrum also presents a strong non-peptide carbonyl (C=O) band at 1739cm−1 and a carbohydrate band at ~1010 cm−1.	2019-10-30	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer		Zenodo	biologists	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer			
03E6B675FFA2345D01CB95E1FA41FD36.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/3748982/files/figure.png	https://doi.org/10.5281/zenodo.3748982	Figure 4. T. rex tissues exhibit positive antibody binding to protein components of extant vascular tissue. (a,c,e,g,i,k,m,o) Are composite images in which fluorescence corresponding to antibody-antigen complexes is overlain upon VLM images of vessel sections, with adjacent images (b,d,f,h,j,l,n,p) captured using a fluorescent filter. (a–d) No spurious binding was observed for negative controls in which vessels were exposed to secondary antibodies raised against the host species of all other antibodies used, i.e., mouse (a,b) and rabbit (c,d). (e,f) Positive binding of dinosaur vessels to actin antibodies can be seen in thin, evenly distributed layers, and (g,h) more broadly distributed binding is apparent for muscle tropomyosin antibodies. Antibodies to both (i,j) type I collagen and (k,l) elastin bind positively to these T. rex vessels. (m,n) Antibodies raised against ostrich haemoglobin exhibit comparatively lower binding intensity. (o,p) No reactivity of dinosaur vessels to antibodies against bacterial peptidoglycan was observed.	Figure 4. T. rex tissues exhibit positive antibody binding to protein components of extant vascular tissue. (a,c,e,g,i,k,m,o) Are composite images in which fluorescence corresponding to antibody-antigen complexes is overlain upon VLM images of vessel sections, with adjacent images (b,d,f,h,j,l,n,p) captured using a fluorescent filter. (a–d) No spurious binding was observed for negative controls in which vessels were exposed to secondary antibodies raised against the host species of all other antibodies used, i.e., mouse (a,b) and rabbit (c,d). (e,f) Positive binding of dinosaur vessels to actin antibodies can be seen in thin, evenly distributed layers, and (g,h) more broadly distributed binding is apparent for muscle tropomyosin antibodies. Antibodies to both (i,j) type I collagen and (k,l) elastin bind positively to these T. rex vessels. (m,n) Antibodies raised against ostrich haemoglobin exhibit comparatively lower binding intensity. (o,p) No reactivity of dinosaur vessels to antibodies against bacterial peptidoglycan was observed.	2019-10-30	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer		Zenodo	biologists	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer			
03E6B675FFA2345D01CB95E1FA41FD36.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/3748986/files/figure.png	https://doi.org/10.5281/zenodo.3748986	Figure 6. X-ray microprobe analysis of iron in the T. rex vascular tissues. (a,b,e) Optical microscope images of vessel tissues and (c,d,f) corresponding iron µ-XRF distribution maps recorded at 10keV.Brighter pixels correspond to higher Fe content. All scale bars are 50µm. Additional elemental maps of regions (a) and (b) can be found in Fig. S5. In (b,d) the vessel structure is not an organic tissue but a mineralised cast rich in Ba and S (see Fig. S5). Such fine-scale variation in preservation underscores the notion that preservation depends on the microenvironment. Numbered white circles indicate locations of Fe µ-XANES analysis.(g) Stacked normalised Fe K-edge extended XANES spectra of spots 0–6. Fits are shown in red dashed lines, with corresponding residuals plotted at the bottom.All spectra match to goethite (α-FeO(OH)) with normalised sum-square values ranging from 0.59 to 1.93·10−4. For comparison, an example set of the iron bearing reference spectra used are displayed in Fig.S7.	Figure 6. X-ray microprobe analysis of iron in the T. rex vascular tissues. (a,b,e) Optical microscope images of vessel tissues and (c,d,f) corresponding iron µ-XRF distribution maps recorded at 10keV.Brighter pixels correspond to higher Fe content. All scale bars are 50µm. Additional elemental maps of regions (a) and (b) can be found in Fig. S5. In (b,d) the vessel structure is not an organic tissue but a mineralised cast rich in Ba and S (see Fig. S5). Such fine-scale variation in preservation underscores the notion that preservation depends on the microenvironment. Numbered white circles indicate locations of Fe µ-XANES analysis.(g) Stacked normalised Fe K-edge extended XANES spectra of spots 0–6. Fits are shown in red dashed lines, with corresponding residuals plotted at the bottom.All spectra match to goethite (α-FeO(OH)) with normalised sum-square values ranging from 0.59 to 1.93·10−4. For comparison, an example set of the iron bearing reference spectra used are displayed in Fig.S7.	2019-10-30	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer		Zenodo	biologists	Elizabeth M. Boatman;Mark B. Goodwin;Hoi-Ying N. Holman;Sirine F akra;Wenxia Zheng;Ronald Gronsky;Mary H. Schweitzer			
