Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ...
Raw, unprocessed SEM data images for Figure 1 of the manuscript: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils. (A) Fibrils from the B. taurus extant long bone control. Prominent banding (~67nm) is present that is characteristic of type-1 collagen pr...
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Online Access: | https://dx.doi.org/10.5061/dryad.8gtht76sq https://datadryad.org/stash/dataset/doi:10.5061/dryad.8gtht76sq |
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ftdatacite:10.5061/dryad.8gtht76sq 2024-02-04T10:03:53+01:00 Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... Anderson, Landon 2022 https://dx.doi.org/10.5061/dryad.8gtht76sq https://datadryad.org/stash/dataset/doi:10.5061/dryad.8gtht76sq en eng Dryad https://www.authorea.com/users/493372/articles/575804-biomolecular-histology-as-a-novel-proxy-for-ancient-dna-and-protein-sequence-preservation Creative Commons Zero v1.0 Universal https://creativecommons.org/publicdomain/zero/1.0/legalcode cc0-1.0 FOS Biological sciences light and scanning electron microscopy collagen type I woolly mammoth Mammuthus primigenius Mammuthus sp. Bos taurus Dataset dataset 2022 ftdatacite https://doi.org/10.5061/dryad.8gtht76sq 2024-01-05T01:14:15Z Raw, unprocessed SEM data images for Figure 1 of the manuscript: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils. (A) Fibrils from the B. taurus extant long bone control. Prominent banding (~67nm) is present that is characteristic of type-1 collagen protein fibrils (Boatman et al., 2019; Gottardi et al., 2016; Lin et al., 1993; Rabotyagova et al., 2008; Tzaphlidou, 2005). (B) Permafrost YG 610.2397 M. primigenius demineralized bone matrix fibrils. An ~67nm banding pattern on the fibrils is also observed but is somewhat less distinct in comparison to that of the extant B. taurus specimen. (C) Observed fibril structures in the temperate MOR 91.72 M. columbi specimen. Fibril banding is generally absent, suggesting the original chemical state of the type-1 collagen fibrils/sequences is substantially altered. ... : An ~200-300 mg fragment of each specimen was demineralized in EDTA (0.5M, pH 8.0) for ~1-3 days, fixed for 1 hour in 2.5% glutaraldehyde (multiple washes in phosphate-buffered saline were performed before and after fixation to remove glutaraldehyde), and dehydrated in a graded series of ethanol incubations (1 hour at 50%, 1 hour 70%, 1 hour 95%, 3x 1 hour 100% ethanol). Post dehydration, specimens were critical point dried (Tousimis Semidri PVT-3), sputter coated (Cressington 108 Auto) with ~70 angstroms of palladium gold metal, and imaged with a Hitachi S-4700 Cold Cathode Field Emission Scanning Electron Microscope. All images were taken at 50,000x magnification and with an accelerating voltage of 15.0kV. Resultant electron microscope images were processed in Adobe Photoshop 2021, using the Levels tool, with a histogram stretch, followed by a gamma adjustment, followed by a second histogram stretch. Sample preparation for ancient specimens was done in a dedicated “ancient” clean lab separate from the ... Dataset permafrost DataCite Metadata Store (German National Library of Science and Technology) |
institution |
Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
English |
topic |
FOS Biological sciences light and scanning electron microscopy collagen type I woolly mammoth Mammuthus primigenius Mammuthus sp. Bos taurus |
spellingShingle |
FOS Biological sciences light and scanning electron microscopy collagen type I woolly mammoth Mammuthus primigenius Mammuthus sp. Bos taurus Anderson, Landon Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
topic_facet |
FOS Biological sciences light and scanning electron microscopy collagen type I woolly mammoth Mammuthus primigenius Mammuthus sp. Bos taurus |
description |
Raw, unprocessed SEM data images for Figure 1 of the manuscript: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils. (A) Fibrils from the B. taurus extant long bone control. Prominent banding (~67nm) is present that is characteristic of type-1 collagen protein fibrils (Boatman et al., 2019; Gottardi et al., 2016; Lin et al., 1993; Rabotyagova et al., 2008; Tzaphlidou, 2005). (B) Permafrost YG 610.2397 M. primigenius demineralized bone matrix fibrils. An ~67nm banding pattern on the fibrils is also observed but is somewhat less distinct in comparison to that of the extant B. taurus specimen. (C) Observed fibril structures in the temperate MOR 91.72 M. columbi specimen. Fibril banding is generally absent, suggesting the original chemical state of the type-1 collagen fibrils/sequences is substantially altered. ... : An ~200-300 mg fragment of each specimen was demineralized in EDTA (0.5M, pH 8.0) for ~1-3 days, fixed for 1 hour in 2.5% glutaraldehyde (multiple washes in phosphate-buffered saline were performed before and after fixation to remove glutaraldehyde), and dehydrated in a graded series of ethanol incubations (1 hour at 50%, 1 hour 70%, 1 hour 95%, 3x 1 hour 100% ethanol). Post dehydration, specimens were critical point dried (Tousimis Semidri PVT-3), sputter coated (Cressington 108 Auto) with ~70 angstroms of palladium gold metal, and imaged with a Hitachi S-4700 Cold Cathode Field Emission Scanning Electron Microscope. All images were taken at 50,000x magnification and with an accelerating voltage of 15.0kV. Resultant electron microscope images were processed in Adobe Photoshop 2021, using the Levels tool, with a histogram stretch, followed by a gamma adjustment, followed by a second histogram stretch. Sample preparation for ancient specimens was done in a dedicated “ancient” clean lab separate from the ... |
format |
Dataset |
author |
Anderson, Landon |
author_facet |
Anderson, Landon |
author_sort |
Anderson, Landon |
title |
Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
title_short |
Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
title_full |
Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
title_fullStr |
Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
title_full_unstemmed |
Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
title_sort |
raw, unprocessed sem data images for: figure 1: scanning electron microscope images of “type-1 bone collagen” demineralized bone matrix fibrils ... |
publisher |
Dryad |
publishDate |
2022 |
url |
https://dx.doi.org/10.5061/dryad.8gtht76sq https://datadryad.org/stash/dataset/doi:10.5061/dryad.8gtht76sq |
genre |
permafrost |
genre_facet |
permafrost |
op_relation |
https://www.authorea.com/users/493372/articles/575804-biomolecular-histology-as-a-novel-proxy-for-ancient-dna-and-protein-sequence-preservation |
op_rights |
Creative Commons Zero v1.0 Universal https://creativecommons.org/publicdomain/zero/1.0/legalcode cc0-1.0 |
op_doi |
https://doi.org/10.5061/dryad.8gtht76sq |
_version_ |
1789971705691635712 |