By T. E. Hardingham (auth.), Struther Arnott, D. A. Rees, E. R. Morris (eds.)
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Accuracy and Precision in Fiber Diffraction Analyses Anyone exploiting a physical probe of molecular structure is under some obligation to provide an assessment of the accuracy of its results and some estimate of their precision. This obligation is more pressing than usual in the case of fiber diffraction studies, which are undertaken by only a few among whom there is no consensus regarding the scope and limits of such studies. What is certainly true is that the number, quality, and resolving power of the X-ray diffraction intensities from fibrous specimens are rarely sufficient for the relative atomic positions in the diffracting molecules to be established independently with useful accuracy.
And -C0 2 - substituents on the chondroitin chains (Fig. 6); every Ca2 + is coordinated to eight oxygen atoms; the number of water molecules making at least two bonding connections with other atoms totals the seven per disaccharide predicted by the density measurements. A major flaw in this procedure is that the initial solution of the phase problem comes from a postulated model, and it is not always the case that the process of refinement can trans form an erroneous model into a refineable one of the correct type.
93 aHelix pitch = h x p (nm); average rotation (t) per disaccharide = 3600 x (q/p). "The pitch ofthe "low h" hyaluronate helices varies somewhat with the cation species present. 'The threefold helices of chondroitin 6-sulfate and of dermatan sulfate are assumed to be left-handed like those of hyaluronate and chondroitin 4-sulfate. d'fhe eightfold helix of chondroitin 6-sulfate has been assumed to be right-handed like that of dermatan sulfate. X-Ray Diffraction Analyses of Glycosaminoglycans 53 These studies of the early 1970s defined the range of glycosaminoglycan secondary structures.