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Situ X-ray Diffraction (situ + x-ray_diffraction)
Selected AbstractsKinetics of Oxidation Processes in the System Co/Ga Studied by in situ X-Ray Diffraction.CHEMINFORM, Issue 50 2003Ulrich Koops Abstract For Abstract see ChemInform Abstract in Full Text. [source] On the Stability of Amorphous Minerals in Lobster CuticleADVANCED MATERIALS, Issue 40 2009Ali Al-Sawalmih In situ X-ray diffraction during heating of lobster cuticle reveals three regions of thermally induced transformations: 1)Chitin decomposition, 2) amorphous calcium carbonate (ACC) , calcite transformation, and 3) amorphous calcium phosphate (ACP) , hydroxyapatite transformation. These results provide new insights into the stabilization mechanisms of amorphous biominerals based on ACC and ACP. [source] In situ X-ray diffraction analysis of (CFx)n batteries: signal extraction by multivariate analysisJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 6 2007Mark A. Rodriguez (CFx)n cathode reaction during discharge has been investigated using in situ X-ray diffraction (XRD). Mathematical treatment of the in situ XRD data set was performed using multivariate curve resolution with alternating least squares (MCR,ALS), a technique of multivariate analysis. MCR,ALS analysis successfully separated the relatively weak XRD signal intensity due to the chemical reaction from the other inert cell component signals. The resulting dynamic reaction component revealed the loss of (CFx)n cathode signal together with the simultaneous appearance of LiF by-product intensity. Careful examination of the XRD data set revealed an additional dynamic component which may be associated with the formation of an intermediate compound during the discharge process. [source] Cyclic olefin homopolymer-based microfluidics for protein crystallization and in situ X-ray diffractionACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2009Soheila Emamzadah Microfluidics is a promising technology for the rapid identification of protein crystallization conditions. However, most of the existing systems utilize silicone elastomers as the chip material which, despite its many benefits, is highly permeable to water vapour. This limits the time available for protein crystallization to less than a week. Here, the use of a cyclic olefin homopolymer-based microfluidics system for protein crystallization and in situ X-ray diffraction is described. Liquid handling in this system is performed in 2,mm thin transparent cards which contain 500 chambers, each with a volume of 320,nl. Microbatch, vapour-diffusion and free-interface diffusion protocols for protein crystallization were implemented and crystals were obtained of a number of proteins, including chicken lysozyme, bovine trypsin, a human p53 protein containing both the DNA-binding and oligomerization domains bound to DNA and a functionally important domain of Arabidopsis Morpheus' molecule 1 (MOM1). The latter two polypeptides have not been crystallized previously. For X-ray diffraction analysis, either the cards were opened to allow mounting of the crystals on loops or the crystals were exposed to X-rays in situ. For lysozyme, an entire X-ray diffraction data set at 1.5,Å resolution was collected without removing the crystal from the card. Thus, cyclic olefin homopolymer-based microfluidics systems have the potential to further automate protein crystallization and structural genomics efforts. [source] | ||||||||||