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43 citations found for Yamamura,

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By combining 1 MeV high-voltage-high-resolution electron microscopy with convergent-beam electron diffraction (CBED), the crystal structure of a perovskite-related compound, Ca4YFe5O13, is determined. The crystal has orthorhombic symmetry with lattice parameters a = 5.46, b = 37.4 and c = 5.54 Å. The space group is determined to be centrosymmetric Pnma by selecting the point group from the CBED patterns. The structure images taken from two principle-axis directions, which are interpreted on the basis of the calculated images, reveal that the structure consists of a succession of the stacking of FeO6 octahedra (O layer) and FeO4 tetrahedra (T layer) and is represented by the stacking sequence of ...OTOOTOTOOTO... along the b axis repeated at intervals of 37.4 Å. It is shown that the Ca4YFe5O13 crystal structure can be described in terms of unit-cell-level twinning of Ca2Fe2O5.

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A monomeric mutant of Azami-Green from G. fascicularis was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal belonged to space group P1 and diffracted X-rays to 2.20 Å resolution.


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The putative sensor histidine kinase domain of the cytoplasmic protein HksP4 from the hyperthermophilic bacterium A. aeolicus VF5 was expressed, purified and crystallized by the sitting-drop vapour-diffusion method. Crystals were obtained in the presence of ATP and AMPPNP; they were found to belong to the same space group P212121 and diffracted X-rays to 3.1 and 2.9 Å resolution, respectively.

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The absolute configuration was determined for the title compound, which was prepared in a synthetic study on the natural products bryostatins. There are two independent mol­ecules which show similar conformations, except for the orientation of the methoxy groups.

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The absolute configuration was determined for the optically active title compound, which was prepared in a synthetic study on the natural products bryostatins.

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Acta Cryst. (2011). A67, C272-C273
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Acta Cryst. (2011). A67, C240
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The first crystal structure of brazzein, the smallest sweet-tasting protein, has been solved at 1.8 Å resolution. The crystal structure possesses an additional [alpha]-helix that was not found in previously reported solution structures and exhibits a different molecular shape from the solution structures, with r.m.s.d.s on C[alpha] atoms of 2.0-2.2 Å.

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Acta Cryst. (2014). A70, C1511
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Brazzein, a 6.5-kDa protein consisting of 54 amino acids and four disulfide bonds, is the smallest sweet-tasting protein yet isolated from the wild African plant Pentadiplandra brazzeana. Brazzein has various desirable properties for use as a low-calorie sweetener in the diets of individuals suffering from diabetes, obesity, and metabolic syndrome. For example, brazzein has a high water solubility and a high thermostability. In addition, brazzein is 2000-times sweeter than sucrose on a weight basis. Both the solution and crystal structures of brazzein have been reported. In the crystal structure [1], brazzein has a defensin-like fold containing two [alpha]-helices and a three-stranded antiparallel [beta]-sheet. Defensins are small cysteine-rich cationic proteins found in both animals and plants, which function by binding to the microbial cell membrane, and, once embedded, forming pore-like membrane defects that allow efflux of essential ions and nutrients. In fact, Yount and Yeaman reported that brazzein has antimicrobial activity against Gram positive (Bacillus subtilis and Staphylococcus aureus) and negative (Escherichia coli) bacteria and a fungus (Candida albicans) at pH 7.5 rather than pH 5.5 [2]. A search for proteins with a similar backbone fold to brazzein using the DALI server shows that structurally similar proteins to brazzein include plant defensins, scorpion neurotoxins (K+ channel blockers), arthropod defensins, mollusc defensins, mold defensins, and a plant trypsin inhibitor. These proteins commonly have a [gamma]-core sequence. Here we compare their sequences, structures and functions, which has led to a conclusion that the C-terminal half of brazzein is important for its antimicrobial activity, brazzein will not have a neurotoxin activity, and it will not act as a trypsin inhibitor.

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Acta Cryst. (2008). A64, C472
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