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16 citations found for Mizohata, E

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The bacterial cell-division protein FtsA from methicillin-resistant S. aureus was crystallized and X-ray diffraction data were collected to a resolution of 2.3 Å.

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A new molecular packing of pseudoazurin from A. faecalis shows a right-handed double helix composed of blue copper sites.

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A structure of a copper-containing nitrite reductase from Geobacillus thermodenitrificans (GtNIR) was determined using an anaerobically manipulated crystal. Furthermore, a peroxide-bound structure of GtNIR was determined.

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The crystal structure of human-heart-type fatty-acid-binding protein in complex with anilinonaphthalene-8-sulfonate was solved at 2.15 Å resolution revealing the detailed binding mechanism of the fluorescent probe 1-anilinonaphthalene-8-sulfonate.


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Glutathione-dependent dehydroascorbate reductase from spinach chloroplasts has been crystallized. The crystals diffract to 2.2 Å and belong to space group C2.

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The UDP-glucuronic acid:flavonol-3-O-glucuronosyltransferase (VvGT5) from the grapevine V. vinifera was purified and crystallized. The best crystal diffracted X-rays to 2.2 Å resolution and belonged to space group P6122.

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Sulfur SAD phasing facilitates the structure determination of diverse native proteins using femtosecond X-rays from free-electron lasers via serial femtosecond crystallography.

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Acta Cryst. (2005). A61, c200
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Aldo-keto reductase 1B3 (AKR1B3) produced in Escherichia coli has been crystallized in complex with NADPH by the sitting-drop vapour-diffusion method.

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Orotate phosphoribosyltransferase from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg2+.

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High-energy X-rays are essential for de novo structure determination with strong anomalous scattering from selenium or mercury. Single-wavelength anomalous diffraction phasing using selenomethionine-derivatization and mercury-soaking techniques has been successfully applied to serial femtosecond crystallography with 13.0 keV or 12.6 keV X-rays produced at SACLA.

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