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...

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Main Author: Anderson, Landon
Format: Other/Unknown Material
Language:unknown
Published: Zenodo 2022
Subjects:
Online Access:https://doi.org/10.5061/dryad.8gtht76sq
id ftzenodo:oai:zenodo.org:7306056
record_format openpolar
spelling ftzenodo:oai:zenodo.org:7306056 2024-09-15T18:30:08+00:00 Raw, unprocessed SEM data images for: Figure 1: Scanning electron microscope images of "type-1 bone collagen" demineralized bone matrix fibrils Anderson, Landon 2022-11-08 https://doi.org/10.5061/dryad.8gtht76sq unknown Zenodo https://www.authorea.com/users/493372/articles/575804-biomolecular-histology-as-a-novel-proxy-for-ancient-dna-and-protein-sequence-preservation https://zenodo.org/communities/dryad https://doi.org/10.5061/dryad.8gtht76sq oai:zenodo.org:7306056 info:eu-repo/semantics/openAccess Creative Commons Zero v1.0 Universal https://creativecommons.org/publicdomain/zero/1.0/legalcode light and scanning electron microscopy collagen type I woolly mammoth Mammuthus primigenius Mammuthus sp Bos taurus info:eu-repo/semantics/other 2022 ftzenodo https://doi.org/10.5061/dryad.8gtht76sq 2024-07-26T15:28:28Z 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. The files are "Tiff" file format, so any program that can open "Tiff" images should be able to open these files for viewing. File 03-03-2022_Cow_Collagen_m01_300dpi.tif corresponds to Figure 1a File 01-21-2022_Woolly_Mammoth_collagen_m01_m02_300dpi.tif corresponds to Figure 1b File 03-14-2022_MOR501_Collagen_m03_300dpi.tif corresponds to Figure 1c Funding provided by: Private Donors (Lynn and Susan Packard Orr; Vance and Gayle Mullis)* Crossref Funder Registry ID: Award Number: Other/Unknown Material permafrost Zenodo
institution Open Polar
collection Zenodo
op_collection_id ftzenodo
language unknown
topic light and scanning electron microscopy
collagen type I
woolly mammoth
Mammuthus primigenius
Mammuthus sp
Bos taurus
spellingShingle 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 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. The files are "Tiff" file format, so any program that can open "Tiff" images should be able to open these files for viewing. File 03-03-2022_Cow_Collagen_m01_300dpi.tif corresponds to Figure 1a File 01-21-2022_Woolly_Mammoth_collagen_m01_m02_300dpi.tif corresponds to Figure 1b File 03-14-2022_MOR501_Collagen_m03_300dpi.tif corresponds to Figure 1c Funding provided by: Private Donors (Lynn and Susan Packard Orr; Vance and Gayle Mullis)* Crossref Funder Registry ID: Award Number:
format Other/Unknown Material
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 Zenodo
publishDate 2022
url https://doi.org/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
https://zenodo.org/communities/dryad
https://doi.org/10.5061/dryad.8gtht76sq
oai:zenodo.org:7306056
op_rights info:eu-repo/semantics/openAccess
Creative Commons Zero v1.0 Universal
https://creativecommons.org/publicdomain/zero/1.0/legalcode
op_doi https://doi.org/10.5061/dryad.8gtht76sq
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