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 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.