Expression, crystallization and preliminary crystallographic studies of a novel bifunctionalN-acetylglutamate synthase/kinase fromXanthomonas campestrishomologous to vertebrateN-acetylglutamate synthase
- 30 November 2006
- journal article
- crystallization communications
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 62 (12) , 1218-1222
- https://doi.org/10.1107/s1744309106044101
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.Keywords
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