Abstract
The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 Å. The crystal belonged to space group P21212, with unit cell parameters a = 57.19 Å, b =94.76 Å, c =47.58 Å. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.
Keywords: Streptococcus mutans, N-acetylglutamate kinase (NAGK), arginine biosynthesis, protein crystallography
Protein & Peptide Letters
Title: Protein Preparation, Crystallization and Preliminary X-Ray Crystallographic Analysis of N-Acetylglutamate Kinase from Streptococcus mutans
Volume: 15 Issue: 5
Author(s): Chang-Wei Wu, Lan-Fen Li, Xiang Liu, Xiong-Zhuo Gao, Jian Lei, Xiao-Dong Su, Xiaojun Zhao and Yu-He Liang
Affiliation:
Keywords: Streptococcus mutans, N-acetylglutamate kinase (NAGK), arginine biosynthesis, protein crystallography
Abstract: The N-acetylglutamate kinase from Streptococcus mutans was expressed in Escherichia coli in soluble form and purified to homogeneity. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.06 Å. The crystal belonged to space group P21212, with unit cell parameters a = 57.19 Å, b =94.76 Å, c =47.58 Å. The gel filtration and initial phasing results showed that the enzyme exists as a monomer, which is different from previously reported N-acetylglutamate kinases.
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Cite this article as:
Wu Chang-Wei, Li Lan-Fen, Liu Xiang, Gao Xiong-Zhuo, Lei Jian, Su Xiao-Dong, Zhao Xiaojun and Liang Yu-He, Protein Preparation, Crystallization and Preliminary X-Ray Crystallographic Analysis of N-Acetylglutamate Kinase from Streptococcus mutans, Protein & Peptide Letters 2008; 15 (5) . https://dx.doi.org/10.2174/092986608784567519
DOI https://dx.doi.org/10.2174/092986608784567519 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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