Fuji Imaging Plate Research Articles

Calibration of imaging plate detectors to mono-energetic protons in the range 1-200 MeV.

Responses of Fuji Imaging Plates (IPs) to proton have been measured in the range 1-200 MeV. Mono-energetic protons were produced with the 15 MV ALTO-Tandem accelerator of the Institute of Nuclear Physics (Orsay, France) and, at higher energies, with the 200-MeV isochronous cyclotron of the Institut Curie-Centre de Protonthérapie d'Orsay (Orsay, France). The experimental setups are described and the measured photo-stimulated luminescence responses for MS, SR, and TR IPs are presented and compared to existing data. For the interpretation of the results, a sensitivity model based on the Monte Carlo GEANT4 code has been developed. It enables the calculation of the response functions in a large energy range, from 0.1 to 200 MeV. Finally, we show that our model reproduces accurately the response of more complex detectors, i.e., stack of high-Z filters and IPs, which could be of great interest for diagnostics of Petawatt laser accelerated particles.

Response functions of Fuji imaging plates to monoenergetic protons in the energy range 0.6–3.2 MeV

We have measured the responses of Fuji MS, SR, and TR imaging plates (IPs) to protons with energies ranging from 0.6 to 3.2 MeV. Monoenergetic protons were produced with the 3.5 MV AIFIRA (Applications Interdisciplinaires de Faisceaux d'Ions en Région Aquitaine) accelerator at the Centre d'Etudes Nucléaires de Bordeaux Gradignan (CENBG). The IPs were irradiated with protons backscattered off a tantalum target. We present the photo-stimulated luminescence response of the IPs together with the fading measurements for these IPs. A method is applied to allow correction of fading effects for variable proton irradiation duration. Using the IP fading corrections, a model of the IP response function to protons was developed. The model enables extrapolation of the IP response to protons up to proton energies of 10 MeV. Our work is finally compared to previous works conducted on Fuji TR IP response to protons.

Absolute response of Fuji imaging plate detectors to picosecond-electron bunches

The characterization of the absolute number of electrons generated by laser wakefield acceleration often relies on absolutely calibrated FUJI imaging plates (IP), although their validity in the regime of extreme peak currents is untested. Here, we present an extensive study on the dependence of the sensitivity of BAS-SR and BAS-MS IP to picosecond electron bunches of varying charge of up to 60 pC, performed at the electron accelerator ELBE, making use of about three orders of magnitude of higher peak intensity than in prior studies. We demonstrate that the response of the IPs shows no saturation effect and that the BAS-SR IP sensitivity of 0.0081 photostimulated luminescence per electron number confirms surprisingly well data from previous works. However, the use of the identical readout system and handling procedures turned out to be crucial and, if unnoticed, may be an important error source.

Visualisation of uric acid renal calculi (UARC) using computed radiography (CR)

Aim To investigate the capability of CR to visualise UARC through inverse image post-processing technique. Methods. A patient-equivalent phantom (PEP) consisting of six 2.5-cm thick Perspex layers and one 1-mm thick aluminium layer was used to represent human tissues and bones respectively. A total of eight exposures were made on PEP to radiograph 1 mm, 2 mm and 3 mm UARC located between three layers of 2-cm thick cattle muscle, positioned inside the PEP. After each exposure, a layer of Perspex was removed, and another exposure was made until only one Perspex layer and one layer of muscle (containing the three UARC) remained. For each exposure, two images (a positive and an inverse image) were produced for comparison using Fuji XG1 computed radiography system with IP0 type C-ST-VI Fuji imaging plate (equivalent to 400 speed radiographic screen-film systems). Results In positive image, UARC of all three sizes (1 mm, 2 mm and 3 mm) located in the cattle muscle, cannot be visualised when the PEP consists of more than one layer of Perspex. In inverse image, the 3-mm UARC can be seen even when the PEP consists of five layers of Perspex. Conclusion This study revealed the post-processing capability of CR to increase the visualisation of UARC which has been categorised as radiolucent. A further study of clinical image quality should be performed using blinded observers to test diagnostic accuracy, which was not included in this study.

New BaBrCl: Eu2+ phosphors for X-ray image recording

Photostimulated luminescence (PSL) is observed in BaBrCl: Eu2+ after X-ray irradiation at room temperature. It is suggested by PSL stimulation spectrum and difference absorption spectrum (DAS) that F centers are formed upon X-ray irradiation and both spectra show two bands which are centered at about 550 nm and 675 nm respectively. This enables the use of semiconductor light-emitting diodes (LED) instead of gas lasers for photostimulation. The PSL intensity increases linearly with X-ray irradiation dose increasing, and the conversion efficiency is 29% that for the standard commercial storage phosphor BaFBr:Eu from Fuji imaging plate.

Serum Amyloid A, but Not C-Reactive Protein, Stimulates Vascular Proteoglycan Synthesis in a Pro-Atherogenic Manner

Inflammatory markers serum amyloid A (SAA) and C-reactive protein (CRP) are predictive of cardiac disease and are proposed to play causal roles in the development of atherosclerosis, in which the retention of lipoproteins by vascular wall proteoglycans is critical. The purpose of this study was to determine whether SAA and/or CRP alters vascular proteoglycan synthesis and lipoprotein retention in a pro-atherogenic manner. Vascular smooth muscle cells were stimulated with either SAA or CRP (1 to 100 mg/L) and proteoglycans were then isolated and characterized. SAA, but not CRP, increased proteoglycan sulfate incorporation by 50 to 100% in a dose-dependent manner (P < 0.0001), increased glycosaminoglycan chain length, and increased low-density lipoprotein (LDL) binding affinity (K(d), 29 microg/ml LDL versus 90 microg/ml LDL for SAA versus control proteoglycans; P < 0.005). Furthermore, SAA up-regulated biglycan via the induction of endogenous transforming growth factor (TGF)-beta. To determine whether SAA stimulated proteoglycan synthesis in vivo, ApoE(-/-) mice were injected with an adenovirus expressing human SAA-1, a null virus, or saline. Mice that received adenovirus expressing SAA had increased TGF-beta concentrations in plasma and increased aortic biglycan content compared with mice that received either null virus or saline. Thus, SAA alters vascular proteoglycans in a pro-atherogenic manner via the stimulation of TGF-beta and may play a causal role in the development of atherosclerosis.

New solutions to the problems of chain orientation and chain continuity in structure analysis of fibrous polymers. A reconsideration of the structure of polyisobutene

Two points of general interest in structural refinement of polymers based on internal coordinates are discussed: the chain orientation and the chain continuity. Using a proprietary computer program, based on revised approaches to these questions, the structure of polyisobutene has been reconsidered, using new X-ray diffraction measurements (Fuji image plate) and performing a structure refinement based on internal coordinates. Three refinement schemes, with a decreasing number of degrees of freedom, have been considered, with the conclusion that the distortion from the 83regular helix, claimed by Tadokoro [(1979).Structure of Crystalline Polymers, p. 136. New York: Wiley-Interscience], is confirmed, though lower than supposed. The new procedures implemented for chain orientation and chain continuity work excellently.

Mutations in the SF1-U2AF59-U2AF23 Complex Cause Exon Skipping in Schizosaccharomyces pombe

To identify genes involved in the mechanism to ensure ordered 5' to 3' exon joining in constitutively spliced pre-mRNAs, we screened for mutants that cause exon skipping in the fission yeast Schizosaccharomyces pombe using a reporter plasmid, which contains the ura4+ gene with the nda3 intron 1-exon 2-intron 2 sequence. The reporter plasmid was designed to produce the functional ura4+ mRNA, when the central nda3 exon is skipped during the splicing reaction. We mutagenized cells harboring the plasmid by UV irradiation and isolated 34 ura+ mutants that grew on minimal medium. Of those, eight mutants were found to be temperature sensitive (ts) for growth. Complementation analyses revealed that the ts mutants belong to three distinct complementation groups named ods (ordered splicing) 1, 2, and 3. RT-PCR analyses showed that products of exon skipping were actually generated in the ods mutants. We cloned the genes responsible for the ods mutations, and found that ods1+, ods2+, and ods3+ encode splicing factors Prp2p/U2AF59, U2AF23, and SF1, respectively, which form a SF1-U2AF59-U2AF23 complex involved in recognition of the branch-point and 3' splice site sequences in a pre-mRNA. We also showed that mutations in the SF1-U2AF59-U2AF23 binding sequences in the reporter plasmid result in exon skipping in wild-type S. pombe cells. In addition, drugs that decrease the rate of transcription elongation were found to suppress the exon skipping in the ods mutants. These results suggest that co-transcriptional recognition of a nascent pre-mRNA by the SF1-U2AF59-U2AF23 complex is essential for ordered exon joining in constitutive splicing in S. pombe.

Benzene; high level quantum chemical calculations, gas electron diffraction pattern recorded on Fuji imaging plates and a method to explore systematic discrepancies which was used to determine an improved sector correction

The C C bond distance in molecular benzene is used by several electron diffraction groups to calibrate the electron wavelength in a gas electron diffraction experiment. It is therefore important to compare the applied r a value against the currently best available ab initio r e result. A high level CCSD(T = Full)/cc-pVTZ calculation, which has proven to give r e distances close to the experimental values, gave r e(C C) = 1.392 Å. When our wavelength calibration distance r a(C C) = 1.3975 Å is corrected for atomic displacements in the curvilinear approach and for anharmonic vibrations, it matches exactly the calculated r e(C C) value. From a B3LYP/cc-pVTZ molecular force field the distance correction terms ( d hn) and the root-mean-square vibration amplitudes were computed both in the linear and the curvilinear approximations. Gas electron diffraction intensities for benzene were registered on Fuji imaging plates. The data are very reproducible and revealed that systematic discrepancies might be present. A method to investigate systematic errors in electron diffraction is proposed. A multiplicative correction likely due to very small errors in the applied sector correction could be estimated. Applying this new correction the agreement is improved due to the high reproducibility of the imaging plates, however, hardly all systematic errors are removed. The agreement is very good and the errors left are unlikely to be caused by the Fuji imaging plate system.

Crystal Structure of Form I of Syndiotactic 1,2-Poly(4-methyl-1,3-pentadiene)

The crystal structure of the form I of syndiotactic 1,2-poly(4-methyl-1,3-pentadiene) has been determined studying the X-ray fiber diffraction pattern recorded onto a Fuji image plate. The chain conformation (T6G2T2G2), previously proposed by Meille et al. on the basis of the identity period, has been confirmed, but with deviations of chain torsion angles from the 60 and 180° values. The crystal system is triclinic, a = 17.513(8) Å, b = 9.117(6) Å, c = 11.251(14) Å, α = 95.20(4)°, β = 98.01(3)°, γ = 92.74(5)°, and V = 1768(3) Å3. The space group is P1̄, with two chains per cell, each formed by six nonequivalent CH2CH[CHC(CH3)2] chemical units. The crystal structure was determined and refined by the least-squares method, keeping bond lengths fixed and assuming that chemically equivalent bond angles are equal to each other. The refined model shows unrealistic values for some side group bond angles, in particular for the angle between methyl groups. Quite satisfactory results are obtained fixing this angle to the value of 122.7°, as suggested by searching the Cambridge Structural Database. Final disagreement indices are R1 = 14.3% and R2 = 15.0%.

Analysis of the Weissenberg diffraction images from Bi2212, using Fuji imaging plate and Synchrotron X-ray

Analysis of the Weissenberg diffraction images from Bi2212, using Fuji imaging plate and Synchrotron X-ray

Precision of measurement of tissue concentrations by RLG.

Existing investigations about the precision of radioluminography (RLG) are restricted to descriptive analysis of the tissue samples. The aim of the present experiments was to obtain a general prospective statement about the precision that the RLG method can achieve. Several pharmaceutical companies in Europe participated in the experiments. Albino rats of various strains were dosed with various (14)C-labeled compounds. Whole-body sections were produced, and blood calibration scales were set up with standard radioactivity sources of dog or rat blood. Photostimulated luminescence was detected using Fuji imaging plate BAS-III. For each organ separately, variability was investigated on each of the levels: rat, section of rat, region within section, and residual, with the help of variance components. The producing company was seen as a fixed factor and adjusted for. A mixed linear model was fitted to the log-transformed data. The variance component (SD estimate) for the residual term gave the desired prospective statement about the achievable precision of the RLG method. Exponential back transformation from the logarithmic to the natural scale transformed the SD estimates to multiplication factors. In total, 29 organs were investigated. The RLG method was comparable in precision to the dissection/combustion method.

Crystalline Structure of Isotactic Poly(vinylcyclobutane) from Fiber Diffraction Spectra

The crystalline structure of isotactic poly(vinylcyclobutane), claimed to be tetragonal, has been revised on the basis of fiber diffraction spectra. The chain symmetry is 41, as already assessed, but the conformation is different (the identity period is 6.91 A and not 6.60 A). The space group is the orthorhombic P212121 with lattice constants a = 17.14 A, b = 8.99 A, and c = 6.91 A. The excellent quality of the oriented samples allowed a full structure analysis and refinement. Integrated diffraction intensities, from a stretched fiber, measured with a Fuji image plate detector, have been utilized in a constrained refinement (the helix was assumed strictly of 41 symmetry and the C−C bond lengths were set to 1.54 A) obtaining a final R index of 15%. The refined chain bond angles are 103 and 107°, and the chain torsion angles are 165 and 273°.

On the correction of reflection intensities recorded on imaging plates for incomplete absorption in the phosphor layer.

When an X-ray beam is incompletely absorbed in the phosphor layer of an imaging plate (IP), a correction for oblique incidence of the beam on the plate becomes imperative. The perpendicular transmission through the phosphor of Fuji imaging plates has been measured as 30% (HR-IIIN plate, conventional source) for 0.707 Å radiation, and 50 and 85% (BASIII plate, synchrotron radiation) for 0.642 and 0.394 Å radiation, respectively. For a given wavelength, the correction factor is a function of the angle between the diffracted beam and the normal to the surface of the plate. For a flat IP, mounted perpendicularly to the incident beam, the correction increases with the 2θ angle of the reflections, but for other orientations of the IP the dependence is more complex.

Monochromatic beam mammography studies using synchrotron radiation (abstract)

Preliminary experiments have been carried out on the X27C R&amp;D beamline at the National Synchrotron Light Source (NSLS) to explore the potential improvement in contrast in breast imaging using monochromatic synchrotron x-rays [R. E. Johnson et al., SPIE (1995) (to be published)]. In our present study, images have been obtained of ACR, contrast detail and anthropomorphic phantoms at 16 to 24 keV. Phantom thickness varied from 42 to 80 mm. Synchrotron images using a Fuji image plate detector and standard mammographic film have been compared to each other and with conventionally produced images. The preliminary results show an improved contrast over the conventional images with lower absorbed dose in the phantoms. The image plate detector was used for our fist experiments because it was readily available and produces digital data. Experiments using an additional analyzer crystal as a scatter rejection element are also underway at the NSLS [D. Chapman, SRI ‘95 (these proceedings)]. We plan to evaluate a variety of detectors and monochromatic beam geometries in order to develop a system that optimizes mammography image contrast and spatial resolution.

Evaluation of phonon scattering in electron diffraction using image plates and electron energy filtering

There have been few studies of thermal diffuse scattering (TDS) by electron diffraction although this scattering is easily observed. The TDS intensity distribution is as a rule strongly anisotropic which can be ascribed to scattering from individual phonon modes. Results reported so far in the literature are all based on qualitative or semi-quantitative use of the observed intensity distributions. However, at present several new methods (energy filters, imaging plate, CCD, digitized film) are available to extract data for detailed quantitative interpretation. In the present work the Zeiss 912 Omega energy filtering microscope has been used, combined with the Fuji Imaging Plate and a low temperature specimen holder. This opens new possibilities both for the study of soft modes and other TDS phenomena related to phase transitions, and also static disorder and order-disorder effects. By comparison with synchrotron work on TDS , crystals may be very much smaller and count rates are much higher. However, multiple scattering and Kikuchi lines may complicate the interpretation unless thin samples are used.

A high-speed data-collection system for large-unit-cell crystals using an imaging plate as a detector

A high-speed data-collection system for large-unit-cell crystals is presented, using the Fuji Imaging Plate as an X-ray detector and a rotating-anode generator as the X-ray source. It is an automatic data-acquisition system that requires almost no manual intervention. The quality of data collected on the system is discussed. Merging R values ranged from 0.04 to 0.05. Compared with a four-circle diffractometer, data reproducibility was better, isomorphous/anomalous Patterson maps were almost identical in quality and data from a small-molecule crystal, cytidine, were of almost the same quality. Protein structures were refinable using the data measured on the system, the final crystallographic R value of the 2.2 Å 3-isopropylmalatedehydrogenase structure being 0.185 and that of the 1.88 Å Flammulina veltipes agglutinin structure being 0.199.

Crystallization and Preliminary X-Ray Structure Analysis of Pigeon Egg-White Lysozyme1

Calcium binding lysozyme from pigeon egg-white was crystallized by the hanging drop vapor diffusion technique using ammonium sulphate as a precipitant. The crystals belong to the orthorhombic system, space group P2(1)2(1)2(1), and have unit cell dimensions of a = 34.2 A, b = 34.8 A, and c = 99.4 A. One asymmetric unit contains one molecule of the pigeon lysozyme. The crystals diffract X-rays at least to 2.0 A resolution and are suitable for high resolution structure analysis. The diffraction data up to 3.0 A resolution were collected with a diffraction image processor, DIP100, using a Fuji imaging plate as an area detector. The structure was solved by the molecular replacement technique and refined to an R factor of 0.216. Least-squares fitting of the main-chains of pigeon egg-white lysozyme with those of chicken egg-white lysozyme and baboon alpha-lactalbumin showed that the main-chain folding of pigeon lysozyme is more similar to that of chicken lysozyme than that of alpha-lactalbumin. The largest differences between the pigeon and chicken lysozymes are in the surface loop regions.

Crystal structure of thermitase at 1.4A˚resolution

The crystal structure of thermitase, a subtilisin-type serine proteinase from Thermoactinomyces vulgaris, was determined by X-ray diffraction at 1.4 A resolution. The structure was solved by a combination of molecular and isomorphous replacement. The starting model was that of subtilisin BPN' from the Protein Data Bank, determined at 2.5 A resolution. The high-resolution refinement was based on data collected using synchrotron radiation with a Fuji image plate as detector. The model of thermitase refined to a conventional R factor of 14.9% and contains 1997 protein atoms, 182 water molecules and two Ca ions. The tertiary structure of thermitase is similar to that of the other subtilisins although there are some significant differences in detail. Comparison with subtilisin BPN' revealed two major structural differences. The N-terminal region in thermitase, which is absent in subtilisin BPN', forms a number of contacts with the tight Ca2+ binding site and indeed provides the very tight binding of the Ca ion. In thermitase the loop of residues 60 to 65 forms an additional (10) beta-strand of the central beta-sheet and the second Ca2+ binding site that has no equivalent in the subtilisin BPN' structure. The observed differences in the Ca2+ binding and the increased number of ionic and aromatic interactions in thermitase are likely sources of the enhanced stability of thermitase.

Instrumentation for Laue diffraction (invited)

Single-crystal x-ray diffraction data can be measured very quickly in Laue geometry compared with monochromatic methods. Alternatively, this gain factor can be used instead to reduce the sample volume for a fixed exposure time. In the latter case especially, there is a critical need to control parasitic scatter in the Laue camera. The use of Laue geometry as a means of quantitative data acquisition required the solution of some fundamental problems. The so-called ‘‘overlapping orders problem’’ has been found not to be limiting. It can be shown that the bulk of the Laue spots are single order, provided dhkl&amp;lt;2dmin where dhkl is the interplanar spacing and dmin is the resolution limit of the data. In addition, empirical wavelength normalization is required. This can be achieved by using the symmetry of the diffraction pattern. The fact that different equivalents occur at different wavelengths means that the differences in these intensities can be used to establish the ‘‘λ curve.’’ Successful wavelength normalization to date has used a relatively broad-band pass. The multiplicity distribution is the histogram of the number of spots of a given order. This distribution is determined by the ratio λmax/λmin (λmax =maximum wavelength, λmin =minimum wavelength in the beam). λmax is determined by the use of any filters in the beamline. λmin is determined either by the spectral curve or a critical cutoff if a mirror is used. A mirror can be usefully introduced to enhance the multiplicity distribution in favor of single wavelength spots or to focus the white beam; so far only vertical focussing has been used. The detector options used to date have been photographic film, Fuji image plate (at Photon Factory)/Kodak storage phosphor (at Cornell) and charge coupled device (CCD) (at Daresbury). It is useful to consider the joint theoretical spatial and energy distribution of spots in defining the detector specification and geometry. To date, we have processed Laue film data successfully. The attraction of using the CCD, even to look at a small portion of the Laue pattern, is to view the diffraction in real time. This will allow tight control of parasitic scatter for microcrystal Laue diffraction and real-time monitoring for time-resolved work. We performed initial experiments using a direct detection CCD imager, and have obtained satisfactory diffraction data on a 40 ms time scale. Results of this work will be presented. In order to assess the efficacy of the Laue method for quantitative crystallography, we have used Laue data from the protein pea lectin and compared it in detail with monochromatic pea lectin data. To assess the use of a vertically focussing mirror, we have successfully used a mercury derivative protein crystal to yield isomorphous and anomalous differences suitable for phase determination. In both the pea lectin and mercury derivative cases, doublet Laue spots were deconvoluted. In the latter case, the data were used in a difference Fourier calculation which showed the mercury peak. Future developments and projections based on multipole sources are given.