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28 citations found for Ishihara,

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Acta Cryst. (2014). A70, C937
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Peptidylarginine deiminase (PAD) is a Ca2+-dependent enzyme that catalyzes the conversion of protein arginine residues to citrulline. Protein citrullination by PAD confers large structural and mechanical effects on the target proteins by altering intermolecular and intramolecular ionic or hydrophobic interactions. Five paralogous genes (PADI1 - 4 and 6) on human chromosome 1p35-36 encode the human PAD isozymes. Among the PADs, PAD3 shows the highest substrate specificity for synthetic and natural substrate. S100A3 is an EF-hand-type Ca2+-binding S100 protein family member that colocalizes with PAD3 in hair cuticular cells. PAD3 converts a symmetric pair of Arg51 residues on an S100A3 dimer surface to citrullines, causing assembly of a homotetramer, but does not convert other arginines. Although this specific citrullination is largely affected by the formation of two intramolecular disulfides in S100A3, it is not clear how the sheltered Arg51 residues is recognized by PAD3. We are aiming structural analysis of the substrate bound forms to elucidate structural factor that PAD3 recognize Arg51 residues only. Although X-ray crystal structures of the PAD4 isozyme and its complexes with substrate peptides have been reported, structural analysis of other PAD isozymes has not yet been conducted. To obtain the crystals of the substrate-complex, we prepared the C646A mutant and the other inactive mutants (D350A, H470A, D472A) of PAD3. We determined the crystal structures of wild-type PAD3, at first. Then, we have tried to determine the structure of the substrate complex with the mutants of PAD3. However, the solved structures did not contain the substrate at present stage. From our structural analysis, only the crystals of C646A were belonged to different crystal system from the others, and its difference didn't relate to their crystallization condition. In this conference, we discuss the origin(s) of the differences in the crystal system of C646 from the others.

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The title compound, C10H10O2, was isolated from Eniconsanthum membranifolium J. Sinclair. There are six independent mol­ecules in the unit cell. Intra­molecular hydrogen bonds from the hydr­oxy H atoms to the carbonyl O atoms are observed in the crystal structure.

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The title compound, also known as salicifoline chloride, C12H20NO2+·Cl, was isolated from Eniconsanthum membranifolium J. Sinclair for X-ray analysis. Salicifoline is hydrogen bonded to a chloride ion via the OH group.

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In the title complex, [Pt(C11H7BrN)(C5H7O2)], two crystallographically non-equivalent dimers stacked by [pi]-[pi] inter­actions are arranged anti­parallel to each other.

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In the crystal structure of the title compound, C17H13NOSe2, the exocyclic C=N double bond has a cis configuration.

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The section method is applied to derive the Penrose pattern and related patterns with a ten- or fivefold axis. These are derived from a four-dimensional decagonal crystal or from a five-dimensional icosahedral crystal as a two-dimensional section. The two descriptions correspond to the three- and four-dimensional ones in the usual superstructure and the Penrose pattern can be regarded as the superstructure in the four-dimensional space. The diffraction intensities and symmetries of these patterns are discussed. The present study indicates that the point group in the quasicrystals is noncrystallographic but (m + d)-reducible similarly to that in incommensurate structures, where m and d are the dimension of the real space and the orthogonal complement to it.

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Mouse S-adenosyl-L-homocysteine hydrolase has been crystallized in the presence of the reaction product adenosine. Diffraction data to 1.55 Å resolution were collected using synchrotron radiation.

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Plans to construct surface-analysis equipment which will be placed on beamline BL24XU of SPring-8 are presented. There are three experimental hutches in BL24XU, which are available simultaneously by using diamond monochromators as beam splitters. The purpose of the surface-analysis equipment is the simultaneous measurement of fluorescent and diffracted X-rays in grazing-incidence geometry. The instrument is equipped with a solid-state detector (SSD) and a flat position-sensitive proportional counter (PSPC) combined with analysing crystals for X-ray fluorescence (XRF) analysis. A curved PSPC and the goniometer that mounts the SSD used for XRF are also installed for X-ray diffraction. X-ray fluorescence holography and polarized X-ray emission spectroscopy modes are available, so three-dimensional images of atomic configurations and also the anisotropic structure of materials will be studied.

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In the title compound, C12H15NOS, the thia­zine ring adopts a sofa conformation. Inter­molecular N-H...O hydrogen bonds link centrosymmetrically related mol­ecules into discrete pairs.

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In the title compound, C17H17NOS, the phenyl ring at position 6 of the thia­zine ring is trans to the hydr­oxy group. The thia­zine ring is in a sofa conformation.

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In the title crystal structure, C18H19NOSe, there are two mol­ecules in the asymmetric unit. Pairs of molecules are linked into a centrosymmetric dimer via inter­molecular O—H...N hydrogen bonds [O...N = 2.872 (2) and 2.893 (2) Å].

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The Hg atoms in the crystal structure of the title compound, (CH6N3)2[HgBr4], are tetra­hedrally coordinated by four Br atoms and the resulting [HgBr4]2- tetra­hedral ions are linked to the [C(NH2)3]+ ions by bromine-hydrogen bonds, forming a three-dimensional network. In the structure, the anions are located on special positions. The two different Hg...Br distances of 2.664 (1) and 2.559 (1) Å observed in the tetra­bromidomercurate unit are due to the connection of Br atoms to different number of H atoms.

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