R factors in X-ray fiber diffraction. III. Asymptotic approximations to largest likely R factors

Author(s):  
R. P. Millane

The largest likely R factor is useful for evaluating the significance of R factors obtained in structure determinations, and is smaller in fiber diffraction than in traditional crystallography. Very simple approximations to functions used to calculate the largest likely R factor in fiber diffraction are derived. For example, the largest R factor (R m) for m overlapping terms is very well approximated by Rm ≃ (2/π)1/2 m -1/2. These are a useful alternative to the exact, but quite complicated, expressions derived previously. More significantly, they provide insight into the behavior of R factors in fiber diffraction and may be useful in further analysis.

Author(s):  
J. M. Paque ◽  
R. Browning ◽  
P. L. King ◽  
P. Pianetta

Geological samples typically contain many minerals (phases) with multiple element compositions. A complete analytical description should give the number of phases present, the volume occupied by each phase in the bulk sample, the average and range of composition of each phase, and the bulk composition of the sample. A practical approach to providing such a complete description is from quantitative analysis of multi-elemental x-ray images.With the advances in recent years in the speed and storage capabilities of laboratory computers, large quantities of data can be efficiently manipulated. Commercial software and hardware presently available allow simultaneous collection of multiple x-ray images from a sample (up to 16 for the Kevex Delta system). Thus, high resolution x-ray images of the majority of the detectable elements in a sample can be collected. The use of statistical techniques, including principal component analysis (PCA), can provide insight into mineral phase composition and the distribution of minerals within a sample.


2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Sachiko Yanagisawa ◽  
Minoru Kubo ◽  
Genji Kurisu ◽  
Shinobu Itoh

To unveil the activation of dioxygen on the copper centre (Cu<sub>2</sub>O<sub>2</sub>core) of tyrosinase, we performed X-ray crystallograpy with active-form tyrosinase at near atomic resolution. This study provided a novel insight into the catalytic mechanism of the tyrosinase, including the rearrangement of copper-oxygen species as well as the intramolecular migration of copper ion induced by substrate-binding.<br>


Biochemistry ◽  
2009 ◽  
Vol 48 (14) ◽  
pp. 3089-3099 ◽  
Author(s):  
Jillian Madine ◽  
Alastair Copland ◽  
Louise C. Serpell ◽  
David A. Middleton

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