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Protein Preparation, Crystallization and Preliminary X-Ray Crystallographic Analysis of N-Acetylglutamate Kinase from Streptococcus mutans

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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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Keywords: N-acetylglutamate kinase (NAGK); Streptococcus mutans; arginine biosynthesis; protein crystallography

Document Type: Research Article

Publication date: June 1, 2008

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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