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• W2090703913 abstract "A novel N-acetylglutamate synthase/kinase bifunctional enzyme of arginine biosynthesis that was homologous to vertebrate N-acetylglutamate synthases was identified in Xanthomonas campestris. The protein was overexpressed, purified and crystallized. The crystals belong to the hexagonal space group P6222, with unit-cell parameters a = b = 134.60, c = 192.11 Å, and diffract to about 3.0 Å resolution. Selenomethionine-substituted recombinant protein was produced and selenomethionine substitution was verified by mass spectroscopy. Multiple anomalous dispersion (MAD) data were collected at three wavelengths at SER-CAT, Advanced Photon Source, Argonne National Laboratory. Structure determination is under way using the MAD phasing method." @default.
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• W2090703913 date "2006-11-30" @default.
• W2090703913 modified "2023-09-27" @default.
• W2090703913 title "Expression, crystallization and preliminary crystallographic studies of a novel bifunctional<i>N</i>-acetylglutamate synthase/kinase from<i>Xanthomonas campestris</i>homologous to vertebrate<i>N</i>-acetylglutamate synthase" @default.
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• W2090703913 doi "https://doi.org/10.1107/s1744309106044101" @default.
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