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Large Crystals (large + crystal)
Selected AbstractsGrowth of big single crystals of a new magnetic superconducting double perovskite Ba2PrRu1,xCuxO6CRYSTAL RESEARCH AND TECHNOLOGY, Issue 2 2006S. M. Rao Abstract Single crystals of Ba2PrRu1,xCuxO6 with x = 0 to 0.2, have been grown from high temperature solutions of a mixture of PbO-PbF2 in the temperature range 1100,1200 °C. Thin crystals with mostly a hexagonal and triangular plate like habit measuring up to 1,2 mm across and 0.1,0.2 mm thick were obtained. The size, quality and morphology of the crystals were improved by varying the solution volume as well as additives like B2O3. Large crystals measuring up to 3 mm across and 0.3 to 0.5 mm thick were obtained with 5,7 wt% solute concentration and 0.51 wt% of B2O3. The ZFC curves exhibit a spin glass like behavior with x = 0 and a superconducting transition at 8 to 11 K depending on x = 0.05 to 0.1. The transition was also influenced by the growth temperature and post growth annealing. Powder x-ray diffraction, EDS and Raman spectroscopic measurements confirm the presence of Cu in the crystals. (© 2006 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2006Adeline Goulet A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13,465,Da), was cloned and expressed in Escherichia coli with an N-terminal His6 tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100,300,nl. Crystals belong to space group P6222 or P6422, with unit-cell parameters a = b = 68.1, c = 132.4,Å. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20,Å for the SeMet-labelled and native protein, respectively. [source] Precipitation diagram and optimization of crystallization conditions at low ionic strength for deglycosylated dye-decolorizing peroxidase from a basidiomyceteACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2005Shinya Saijo The growth of suitably sized protein crystals is essential for protein structure determination by X-ray crystallography. In general, crystals are grown using a trial-and-error method. However, these methods have been modified with the advent of microlitre dispensing-robot technology and of protocols that rapidly screen for crystal nucleation conditions. The use of one such automatic dispenser for mixing protein drops (1.3,2.0,µl in volume) of known concentration and pH with precipitating solutions (ejecting 2.0,µl droplets) containing salt is described here. The results of the experiments are relevant to a crystallization approach based on a two-step procedure: screening for the crystal nucleation step employing robotics followed by optimization of the crystallization conditions using incomplete factorial experimental design. Large crystals have successfully been obtained using quantities as small as 3.52,mg protein. [source] A comparison of a microfocus X-ray source and a conventional sealed tube for crystal structure determinationJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 5 2009Thomas Schulz Experiments are described in which a direct comparison was made between a conventional 2,kW water-cooled sealed-tube X-ray source and a 30,W air-cooled microfocus source with focusing multilayer optics, using the same goniometer, detector, radiation (Mo,K,), crystals and software. The beam characteristics of the two sources were analyzed and the quality of the resulting data sets compared. The Incoatec Microfocus Source (IµS) gave a narrow approximately Gaussian-shaped primary beam profile, whereas the Bruker AXS sealed-tube source, equipped with a graphite monochromator and a monocapillary collimator, had a broader beam with an approximate intensity plateau. Both sources were mounted on the same Bruker D8 goniometer with a SMART APEX II CCD detector and Bruker Kryoflex low-temperature device. Switching between sources simply required changing the software zero setting of the 2, circle and could be performed in a few minutes, so it was possible to use the same crystal for both sources without changing its temperature or orientation. A representative cross section of compounds (organic, organometallic and salt) with and without heavy atoms was investigated. For each compound, two data sets, one from a small and one from a large crystal, were collected using each source. In another experiment, the data quality was compared for crystals of the same compound that had been chosen so that they had dimensions similar to the width of the beam. The data were processed and the structures refined using standard Bruker and SHELX software. The experiments show that the IµS gives superior data for small crystals whereas the diffracted intensities were comparable for the large crystals. Appropriate scaling is particularly important for the IµS data. [source] Diffraction cartography: applying microbeams to macromolecular crystallography sample evaluation and data collectionACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2010Matthew W. Bowler Crystals of biological macromolecules often exhibit considerable inter-crystal and intra-crystal variation in diffraction quality. This requires the evaluation of many samples prior to data collection, a practice that is already widespread in macromolecular crystallography. As structural biologists move towards tackling ever more ambitious projects, new automated methods of sample evaluation will become crucial to the success of many projects, as will the availability of synchrotron-based facilities optimized for high-throughput evaluation of the diffraction characteristics of samples. Here, two examples of the types of advanced sample evaluation that will be required are presented: searching within a sample-containing loop for microcrystals using an X-ray beam of 5,µm diameter and selecting the most ordered regions of relatively large crystals using X-ray beams of 5,50,µm in diameter. A graphical user interface developed to assist with these screening methods is also presented. For the case in which the diffraction quality of a relatively large crystal is probed using a microbeam, the usefulness and implications of mapping diffraction-quality heterogeneity (diffraction cartography) are discussed. The implementation of these techniques in the context of planned upgrades to the ESRF's structural biology beamlines is also presented. [source] A comparison of a microfocus X-ray source and a conventional sealed tube for crystal structure determinationJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 5 2009Thomas Schulz Experiments are described in which a direct comparison was made between a conventional 2,kW water-cooled sealed-tube X-ray source and a 30,W air-cooled microfocus source with focusing multilayer optics, using the same goniometer, detector, radiation (Mo,K,), crystals and software. The beam characteristics of the two sources were analyzed and the quality of the resulting data sets compared. The Incoatec Microfocus Source (IµS) gave a narrow approximately Gaussian-shaped primary beam profile, whereas the Bruker AXS sealed-tube source, equipped with a graphite monochromator and a monocapillary collimator, had a broader beam with an approximate intensity plateau. Both sources were mounted on the same Bruker D8 goniometer with a SMART APEX II CCD detector and Bruker Kryoflex low-temperature device. Switching between sources simply required changing the software zero setting of the 2, circle and could be performed in a few minutes, so it was possible to use the same crystal for both sources without changing its temperature or orientation. A representative cross section of compounds (organic, organometallic and salt) with and without heavy atoms was investigated. For each compound, two data sets, one from a small and one from a large crystal, were collected using each source. In another experiment, the data quality was compared for crystals of the same compound that had been chosen so that they had dimensions similar to the width of the beam. The data were processed and the structures refined using standard Bruker and SHELX software. The experiments show that the IµS gives superior data for small crystals whereas the diffracted intensities were comparable for the large crystals. Appropriate scaling is particularly important for the IµS data. [source] On the efficient evaluation of Fourier patterns for nanoparticles and clustersJOURNAL OF COMPUTATIONAL CHEMISTRY, Issue 9 2006Antonio Cervellino Abstract Samples made of an isotropically oriented ensemble of atomic clusters or structures that are not large crystals (i.e. extended less than 10 periods in each direction) are at the frontier of today's material science and chemistry. Examples are nanoparticles, nanotubes, amorphous matter, polymers, and macromolecules in suspension. For such systems the computation of powder diffraction patterns (which may provide an efficient characterization) is to be performed the hard way, by summing contributions from each atom pair. This work deals with performing such computation in the most practical and efficient way. Three main points are developed: how to encode the enormous array of interatomic distances (which increase as the square or higher powers of the cluster diameter) to a much smaller array of equispaced values on a coarse grid (whose size increases linearly with the diameter); how to perform a fast computation of the diffraction pattern from this equispaced grid; how to optimize the grid step to obtain an arbitrarily small error on the computed diffraction pattern. Theory and examples are jointly developed and presented. © 2006 Wiley Periodicals, Inc. J Comput Chem 27: 995,1008, 2006 [source] Factors Dominating Adhesion of NaCl onto Potato ChipsJOURNAL OF FOOD SCIENCE, Issue 8 2007V.E. Buck ABSTRACT:, In this study, the adhesion factors examined were time between frying and coating, surface oil content, chip temperature, oil composition, NaCl size, NaCl shape, and electrostatic coating. Three different surface oil content potato chips, high, low, and no, were produced. Oils used were soybean, olive, corn, peanut, and coconut. After frying, chips were coated immediately, after 1 d, and after 1 mo. NaCl crystals of 5 different particle sizes (24.7, 123, 259, 291, and 388 ,m) were coated both electrostatically and nonelectrostatically. Adhesion of cubic, dendritic, and flake crystals was examined. Chips were coated at different temperatures. Chips with high surface oil had the highest adhesion of salt, making surface oil content the most important factor. Decreasing chip temperature decreased surface oil and adhesion. Increasing time between frying and coating reduced adhesion for low surface oil chips, but did not affect high and no surface oil chips. Changing oil composition did not affect adhesion. Increasing salt size decreased adhesion. Salt size had a greater effect on chips with lower surface oil content. When there were significant differences, cubic crystals gave the best adhesion followed by flake crystals then dendritic crystals. For high and low surface oil chips, electrostatic coating did not change adhesion of small size crystals but decreased adhesion of large salts. For no surface oil content chips, electrostatic coating improved adhesion for small salt sizes but did not affect adhesion of large crystals. [source] Particle Characteristics of Trace High Explosives: RDX and PETN,JOURNAL OF FORENSIC SCIENCES, Issue 2 2007Jennifer R. Verkouteren M.S. ABSTRACT: The sizes of explosives particles in fingerprint residues produced from C-4 and Semtex-1A were investigated with respect to a fragmentation model. Particles produced by crushing crystals of RDX and PETN were sized by using scanning electron microscopy, combined with image analysis, and polarized light microscopy was used for imaging and identifying explosive particles in fingerprint residues. Crystals of RDX and PETN fragment in a manner that concentrates mass in the largest particles of the population, which is common for a fragmentation process. Based on the fingerprints studied, the particle size to target for improving mass detection in fingerprint residues by ion mobility spectrometry (IMS) is ,10 ,m in diameter. Although particles smaller than 10 ,m in diameter have a higher frequency, they constitute <20% of the total mass. Efforts to improve collection efficiency of explosives particles for detection by IMS, or other techniques, must take into consideration that the mass may be concentrated in a relatively few particles that may not be homogeneously distributed over the fingerprint area. These results are based on plastic-bonded explosives such as C-4 that contain relatively large crystals of explosive, where fragmentation is the main process leading to the presence of particles in the fingerprint residues. [source] Protein crystal growth with a two-liquid system and stirring solutionJOURNAL OF SYNCHROTRON RADIATION, Issue 1 2004Hiroaki Adachi We developed two novel methods for growing large, high-quality protein crystals. A two-liquid system enables the convenient extraction of protein crystals without causing mechanical damage due to growth at the interface between two liquids. Since this system does not require limitations on solution volume, it is also suitable for the seed technique, and for growing large crystals. Another new concept is the mild stirring of the solution using the Floating And Stirring Technique (FAST) and the Micro-stirring technique. When compared to conventional techniques, both techniques result in a reduced number of crystals, as well as the growth of large crystals. [source] Nitrogen in diamond-free ureilite Allan Hills 78019: Clues to the origin of diamond in ureilitesMETEORITICS & PLANETARY SCIENCE, Issue 8 2002V. K. Rai A small amount of amorphous carbon combusting at ,500 °C carries most of the noble gases, while the major carbon phase consisting of large crystals of graphite combusts at ,800 °C, and is almost noble-gas free. Nitrogen on the other hand is present in both amorphous carbon and graphite, with different ,15N signatures of ,21%o and +19%o, respectively, distinctly different from the very light nitrogen (about ,100%o) of ureilite diamond. Amorphous carbon in ALH 78019 behaves similar to phase Q of chondrites with respect to noble gas release pattern, behavior towards oxidizing acids as well as nitrogen isotopic composition. In situ conversion of amorphous carbon or graphite to diamond through shock would require an isotopic fractionation of 8 to 12% for nitrogen favoring the light isotope, an unlikely proposition, posing a severe problem for the widely accepted shock origin of ureilite diamond. [source] Mechanism of Formation of Human Calcium Oxalate Renal Stones on Randall's PlaqueTHE ANATOMICAL RECORD : ADVANCES IN INTEGRATIVE ANATOMY AND EVOLUTIONARY BIOLOGY, Issue 10 2007Andrew P. Evan Abstract Although calcium oxalate (CaOx) renal stones are known to grow attached to renal papillae, and specifically to regions of papillae that contain Randall's plaque (interstitial apatite deposits), the mechanisms of stone overgrowth on plaque are not known. To investigate the problem, we have obtained biopsy specimens from two stone patients that included an attached stone along with its tissue base and have studied the ultrastructural features of the attachment point using light and transmission electron microscopy, Fourier transform infrared spectroscopy (,-FTIR), and immunohistochemical analysis. The epithelium is disrupted at the attachment site. The denuded plaque that borders on the urinary space attracts an envelope of ribbon-like laminates of crystal and organic matrix arising from urine ions and molecules. Into the matrix of this ribbon grow amorphous apatite crystals that merge with and give way to the usual small apatite crystals imbedded in stone matrix; eventually CaOx crystals admix with apatite and become the predominant solid phase. Over time, urine calcium and oxalate ions gradually overgrow on the large crystals forming the attached stone. Anat Rec, 290:1315-1323, 2007. © 2007 Wiley-Liss, Inc. [source] Diffraction cartography: applying microbeams to macromolecular crystallography sample evaluation and data collectionACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2010Matthew W. Bowler Crystals of biological macromolecules often exhibit considerable inter-crystal and intra-crystal variation in diffraction quality. This requires the evaluation of many samples prior to data collection, a practice that is already widespread in macromolecular crystallography. As structural biologists move towards tackling ever more ambitious projects, new automated methods of sample evaluation will become crucial to the success of many projects, as will the availability of synchrotron-based facilities optimized for high-throughput evaluation of the diffraction characteristics of samples. Here, two examples of the types of advanced sample evaluation that will be required are presented: searching within a sample-containing loop for microcrystals using an X-ray beam of 5,µm diameter and selecting the most ordered regions of relatively large crystals using X-ray beams of 5,50,µm in diameter. A graphical user interface developed to assist with these screening methods is also presented. For the case in which the diffraction quality of a relatively large crystal is probed using a microbeam, the usefulness and implications of mapping diffraction-quality heterogeneity (diffraction cartography) are discussed. The implementation of these techniques in the context of planned upgrades to the ESRF's structural biology beamlines is also presented. [source] Reducing radiation damage in macromolecular crystals at synchrotron sourcesACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2009Edward A. Stern A new strategy is presented to reduce primary X-ray damage in macromolecular crystallography. The strategy is based on separating the diffracting and damaged regions as much as feasible. The source of the radiation damage to macromolecular crystals is from two primary mechanisms: the direct excitations of electrons by absorption, and inelastic scattering of the X-rays. The first produces photoelectrons with their accompanying Auger electrons from relaxation of the core hole and the second creates Compton electrons. The properties of these two mechanisms and calculations of primary X-ray damage quantify how to modify the spatial distribution of X-rays to reduce the deleterious effects of radiation damage. By focusing the incident X-rays into vertical stripes, it is estimated that the survival (the time during which quality diffraction data can be obtained with a given X-ray flux) of large crystals can be increased by at least a factor of 1.6, while for very small platelet crystals the survival can be increased by up to a factor of 14. [source] Protein crystallization in hydrogel beadsACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2005Ronnie Willaert The use of hydrogel beads for the crystallization of proteins is explored in this contribution. The dynamic behaviour of the internal precipitant, protein concentration and relative supersaturation in a gel bead upon submerging the bead in a precipitant solution is characterized theoretically using a transient diffusion model. Agarose and calcium alginate beads have been used for the crystallization of a low-molecular-weight (14.4,kDa, hen egg-white lysozyme) and a high-molecular-weight (636.0,kDa, alcohol oxidase) protein. Entrapment of the protein in the agarose-gel matrix was accomplished using two methods. In the first method, a protein solution is mixed with the agarose sol solution. Gel beads are produced by immersing drops of the protein,agarose sol mixture in a cold paraffin solution. In the second method (which was used to produce calcium alginate and agarose beads), empty gel beads are first produced and subsequently filled with protein by diffusion from a bulk solution into the bead. This latter method has the advantage that a supplementary purification step is introduced (for protein aggregates and large impurities) owing to the diffusion process in the gel matrix. Increasing the precipitant, gel concentration and protein loading resulted in a larger number of crystals of smaller size. Consequently, agarose as well as alginate gels act as nucleation promoters. The supersaturation in a gel bead can be dynamically controlled by changing the precipitant and/or the protein concentration in the bulk solution. Manipulation of the supersaturation allowed the nucleation rate to be varied and led to the production of large crystals which were homogeneously distributed in the gel bead. [source] | |||||||||||||