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35 citations found for Ohtsuka,

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A novel type of phosphoserine phosphatase from H. thermophilus TK-6 was heterologously expressed in E. coli, purified and crystallized by the sitting-drop vapour-diffusion method. The crystals obtained belonged to space group P212121 and diffracted X-rays to 1.5 Å resolution.

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Acta Cryst. (2014). A70, C450
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A novel haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58 belongs to the HLD-II subfamily and hydrolyzes brominated and iodinated compounds, leading to the generation of the corresponding alcohol, a halide ion, and a proton. DatA possesses a unique Asn-Tyr residue pair instead of the Asn-Trp residue pair conserved among the subfamily members, thus the structural basis for its reaction mechanism merits elucidation. In addition, DatA is potentially useful for pharmaceutical and environmental applications, though several crystal structures of HLD-II dehalogenases have been reported so far, the determination of the DatA structure will provide an important contribution to those fields. This work provided insight into the reaction mechanism of DatA via a combination of X-ray crystallographic and computational analysis. The crystal structures of DatA and the Y109W mutant were determined at 1.70 Å [1] and 1.95 Å, respectively. The location of the active site was confirmed by using its novel competitive inhibitor, CHES. The structural information from these two crystal structures and the docking simulation with 1,3-dibromopropane revealed that the replacement of the Asn-Tyr pair with the Asn-Trp pair increases the binding affinity for 1,3-dibromopropane, due to the extra hydrogen bond between Trp109 and halogenated compounds; and that the key residue to bind halogenated substrate is only Asn43 in the wild-type DatA, while those in the Y109W mutant are the Asn-Trp pair. Furthermore, docking simulation using the crystal structures of DatA and some chiral compounds indicated that enantioselectivity of DatA toward brominated alkanes is determined by the large and small spaces around the halogen binding site.


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A two-dimensional clinical intravenous coronary angiography system, comprising a large-size view area produced by asymmetrical reflection from a silicon crystal using intense synchrotron radiation from a multipole wiggler and a two-dimensional detector with an image intensifier, has been completed. An advantage of the imaging system is that two-dimensional dynamic imaging of the cardiovascular system can be achieved due to its two-dimensional radiation field. This world-first two-dimensional system has been successfully adapted to clinical applications. Details of the imaging system are described in this paper.

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A putative ribosomal RNA-processing factor consisting of two KH domains from Pyrococcus horikoshii OT3 (PH1566; 25 kDa) was crystallized by the sitting-drop vapour-diffusion method using PEG 3000 as the precipitant. The space group of the crystals was determined as primitive orthorhombic P212121, with unit-cell parameters a = 45.9, b = 47.4, c = 95.7 Å.

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The relative configuration was determined for the title compound, which was prepared in a synthetic study on immunosuppressant FR65814. There is an intramolecular hydrogen bond between the hydroxy and epoxy groups.



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It is found that the intensities of bright spots in a spherical aberration (Cs)-uncorrected high-angle annular dark-field (HAADF) scanning transmission electron microscope (STEM) image of [011]-oriented Co3O4 change with sample thickness. From an analysis based on the Bloch-wave theorem, it is found that an insufficient semiangle of the incident convergent beam leads to intensities that do not depend on the average atomic number in the atomic columns.

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The haloalkane dehalogenase DatA from A. tumefaciens C58 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.70 Å resolution.

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Acta Cryst. (1993). A49, c135
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Three-dimensional structures of Escherichia coli overexpressing a metalloprotein ferritin were visualized by synchrotron radiation microtomography.






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Acta Cryst. (2014). A70, C214
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AdpA is the central transcriptional factor in the A-factor regulatory cascade of Streptomyces griseus and activates hundreds of genes required for both secondary metabolism and morphological differentiation, leading to onset of streptomycin biosynthesis as well as aerial mycelium formation and sporulation. It has been shown that AdpA binds to over 500 operator regions with the loosely conserved consensus sequence, 5'-TGGCSNGWWY-3' (S: G or C; W: A or T; Y: T or C; and N: any nucleotide). However, it is still obscure how AdpA can control hundreds of genes. To reveal the molecular basis of the low nucleotide sequence specificity, we have determined the crystal structure of the complex of DNA-binding domain of AdpA and a 14-mer duplex DNA with two-nucleotide overhangs at 5'-ends at 2.95-Å resolution. The crystal structure and electrophoretic mobility-shift assays showed that only two arginine residues, Arg262 and Arg266, are involved in the sequence recognition and determine the nucleotide specificity/preference of continuous five base-pairs of positions 1-5 in the consensus sequence. These results partially explain how AdpA directly controls hundreds of genes.

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Nonlocality in spherical-aberration-corrected high-angle annular dark-field scanning transmission electron microscope images is theoretically and experimentally examined. A detailed comparison between experimental data and simulations suggests that nonlocality in the thermal diffuse scattering absorption potential cannot be ignored for detailed analysis of materials consisting of several heavy elements.

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