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Your search keyword '"Nishitani, Yuichi"' showing total 4 results
Start Over Author "Nishitani, Yuichi" Journal acta crystallographica section f structural biology and crystallization communications
4 results on '"Nishitani, Yuichi"'

3. Purification, crystallization and preliminary X-ray diffraction studies of UDP-N-acetylglucosamine pyrophosphorylase from Candida albicans.

Author

Maruyama D, Nishitani Y, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, and Miki K

Subjects
Crystallization, Crystallography, X-Ray, Nucleotidyltransferases isolation & purification, Candida albicans enzymology, Nucleotidyltransferases chemistry
Abstract

UDP-N-acetylglucosamine pyrophosphorylase (UAP) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine. UAP from Candida albicans was purified and crystallized by the sitting-drop vapour-diffusion method. The crystals of the substrate and product complexes both diffract X-rays to beyond 2.3 A resolution using synchrotron radiation. The crystals of the substrate complex belong to the triclinic space group P1, with unit-cell parameters a = 47.77, b = 62.89, c = 90.60 A, alpha = 90.01, beta = 97.72, gamma = 92.88 degrees, whereas those of the product complex belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 61.95, b = 90.87, c = 94.88 A.

Published
2006
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4. Purification, crystallization and preliminary X-ray diffraction studies of N-acetylglucosamine-phosphate mutase from Candida albicans.

Author

Nishitani Y, Maruyama D, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, and Miki K

Subjects
Crystallization, Phosphotransferases (Phosphomutases) isolation & purification, Recombinant Proteins chemistry, Recombinant Proteins isolation & purification, Synchrotrons, X-Ray Diffraction, Candida albicans enzymology, Phosphotransferases (Phosphomutases) chemistry
Abstract

N-acetylglucosamine-phosphate mutase (AGM1) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) in eukaryotes and belongs to the alpha-D-phosphohexomutase superfamily. AGM1 from Candida albicans (CaAGM1) was purified and crystallized by the sitting-drop vapour-diffusion method. The crystals obtained belong to the primitive monoclinic space group P2(1), with unit-cell parameters a = 60.2, b = 130.2, c = 78.0 angstroms, beta = 106.7 degrees. The crystals diffract X-rays to beyond 1.8 angstroms resolution using synchrotron radiation.

Published
2006
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