European Synchrotron Radiation Facility

About: European Synchrotron Radiation Facility is a nonprofit organization based out in Grenoble, Rhône-Alpes, France. It is known for research contribution in the topics: Scattering & Diffraction. The organization has 3661 authors who have published 10305 publications receiving 332591 citations. The organization is also known as: ESRF.

Two-dimensional detector software: From real detector to idealised image or two-theta scan

Abstract: Detector systems introduce distortions into acquired data. To obtain accurate angle and intensity information, it is necessary to calibrate, and apply corrections. Intensity non-linearity, spatial distortion, and non-uniformity of intensity response, are the primary considerations. It is better to account for the distortions within scientific analysis software, but often it is more practical to correct the distortions to produce ‘idealised’ data. Calibration methods and software have been developed for single crystal diffraction experiments, using both approaches. For powder diffraction experiments the additional task of converting a two-dimensional image to a one-dimensional spectrum is used to allow Rietveld analysis. This task may be combined with distortion correction to produce intensity information and error estimates. High-pressure experiments can introduce additional complications and place new demands on software. Flexibility is needed to be able to integrate different angular regions se...

X-ray circular-dichroism as a probe of orbital magnetization

Abstract: A new magneto-optical sum rule is derived for circular magnetic dichroism in the x-ray region (CMXD). The integral of the CMXD signal over a given edge allows one to determine the ground-state expectation value of the orbital angular momentum. Applications are discussed to transition-metal and rare-earth magnetic systems.

Atomic structures of amyloid cross-beta spines reveal varied steric zippers.

Abstract: Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry ‘steric zipper’. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer’s amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains. Degenerative diseases such as Alzheimer's and Parkinson's are associated with the precipitation of amyloid fibrils in the brain. The fibrils are remarkably uniform in structure, considering the diversity of the proteins that produce them. Sawaya et al. have now identified 30 short fibril-forming peptides taken from a large range of amyloid diseases and have solved the atomic structures of crystals formed by 13 of them. All the peptides so far examined self-assemble by forming variants of the 'steric zipper', a structural feature first found in the yeast prion protein Sup 35. The zipper may be a key to the strength of amyloid fibrils, and is a prime target for therapeutic intervention. Degenerative diseases such as Alzheimer's or Parkinson's are associated with the misfolding of many diverse proteins, yet the amyloid fibrils formed by all these proteins are similar. David Eisenberg and colleagues have now identified 30 short fibril-forming peptides implicated in a range of amyloid diseases and have solved 13 of their atomic structures, revealing variations in one common feature — the 'steric zipper'.

Structure of the cross-beta spine of amyloid-like fibrils.

Abstract: Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-β spine. It is a double β-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.