Manufacturing an active X-ray mirror prototype in thin glass.

Adjustable mirrors equipped with piezo actuators are commonly used at synchrotron and free-electron laser (FEL) beamlines, in order to optimize their focusing properties and sometimes to shape the intensity distribution of the focal spot with the desired profile. Unlike them, X-ray mirrors for astronomy are much thinner in order to enable nesting and reduce the areal mass, and the application of piezo actuators acting normally to the surface appears much more difficult. There remains the possibility to correct the deformations using thin patches that exert a tangential strain on the rear side of the mirror: some research groups are already at work on this approach. The technique reported here relies on actively integrating thin glass foils with commercial piezoceramic patches, fed by voltages driven by the feedback provided by X-rays, while the tension signals are carried by electrodes on the back of the mirror, obtained by photolithography. Finally, the shape detection and the consequent voltage signal to be provided to the piezoelectric array will be determined by X-ray illumination in an intra-focal setup at the XACT facility. In this work, the manufacturing steps for obtaining a first active mirror prototype are described.

Resonance Raman microspectroscopic characterization of eosinophil peroxidase in human eosinophilic granulocytes.

A resonance Raman microspectroscopic study is presented of eosinophil peroxidase (EPO) in human eosinophilic granulocytes. Experiments were carried out at the single cell level with laser excitation in Soret-, Qv-, and charge transfer absorption bands of the active site heme of the enzyme. The Raman signal obtained from the cells was almost exclusively due to EPO. Methods were developed to determine depolarization ratios and excitation profiles of Raman bands of EPO in situ. A number of Raman band assignments based on earlier experiments with isolated EPO have been revised. The results show that in agreement with literature on isolated eosinophil peroxidase, the prosthetic group of the enzyme in the (unactivated) cells is a high spin, 6-coordinated, ferric protoporphyrin IX. The core size of the heme is about 2.04 A. The proximal and distal axial ligands are most likely a histidine with the strong imidazolate character typical for peroxidases, and a weakly bound water molecule, respectively. The data furthermore indicate that the central iron is displaced from the plane of the heme ring. The unusual low wavenumber Raman spectrum of EPO, strongly resembling that of lactoperoxidase, intestinal peroxidase and myeloperoxidase, suggests that these mammalian peroxidases are closely related, and characterized by, as yet unspecified, interactions between the peripheral substituents and the protein, different from those found in other protoheme proteins.