8798 ( N - 77-21214 ) The stress corrosion resistance and the cryogenic. The red and blue colored lines/symbols were measured on. Transmission electron microscopy and x - ray diffuse scattering have been used. The scan step was 0.4 m, and then a single scan took 210 s to measure 40 pulse points. Dive into the research topics of New high- and low-temperature apparatus for synchrotron polycrystalline X-ray diffraction. X-ray intensity was averaged for 10 measurements. Abstract We have developed an experimental apparatus named KOTOBUKI-1 for use in coherent X-ray diffraction imaging experiments of frozen-hydrated non-crystalline particles at cryogenic temperature. Protein crystals and the surrounding mother liquor have high water content, which can lead to ice formation when samples are cooled to cryogenic temperatures. 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. X-ray intensity monitored using a PIN photodiode downstream was normalized using the incident x-ray intensity monitored upstream of KOTOBUKI-1. X-ray diffraction from protein crystals is routinely measured at cryogenic temperatures, primarily to minimize radiation damage. Targets include cells and cell organelles. 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. Coherent X-ray diffraction imaging at cryogenic temperature (cryo-CXDI) allows the analysis of internal structures of unstained, non-crystalline, whole biological samples in micrometre to sub-micrometre dimensions. 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. 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. 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. We present a strip transition-edge sensor microcalorimeter linear array detector developed for energy dispersive X-ray diffraction imaging and Compton. 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.
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