![]() Our products can be found across the world in laboratories conducting cutting-edge research. We envisage that the combination of experimental and modelling approaches could allow mechanical phenotyping at the collagen fibril level of virtually any alteration of collagen structure or chemistry. Cryogenic Devices Sample Cooling Made Simple With over 35 years of experience, we are one of the leading providers of cryogenic devices for use in X-ray diffraction. Our experimental and atomistic simulation results show how the structure and mechanics are altered at the individual collagen fibril level as a result of collagen gene mutation in OIM. These mechanical changes were accompanied by an impaired swelling upon hydration within PBS. Comparing results from atomic force microscopy imaging and cantilever-based nanoindentation on collagen fibrils from OIM and wild-type (WT) animals, we found a 33% lower indentation modulus in OIM when air-dried (bound water present) and an almost fivefold higher indentation modulus in OIM collagen fibrils when fully hydrated (bound and unbound water present) in phosphate-buffered saline solution (PBS) compared with WT collagen fibrils. The polymer specimen could be cooled down to 18 K using this apparatus. As this substitution severely impairs the structure and mechanics of collagen-rich tissues at the tissue and organ level, the main aim of this study was to investigate how the structure and mechanics are altered in OIM collagen fibrils. An x-ray diffraction apparatus, consisting of a load cell, a stretching device, and a cryogenic cell, has been constructed to observe the mechanical deformation of the crystal lattice of polymers at cryogenic temperature. ![]() However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the substitution of the α2(I) chain by one α1(I) chain. Coherent X-ray diffraction imaging at cryogenic temperature (cryo-CXDI) allows the analysis of internal structures of unstained, non-crystalline, whole biologicalsamplesinmicrometretosub-micrometredimensions.Targetsinclude cells and cell organelles. The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. K.D.Irwin, G.C.Hilton, Preprint of chapter in Cryogenic Particle Detection.
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