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  • Title: Protein preparation and preliminary X-ray crystallographic analysis of a putative glucosamine 6-phosphate deaminase from Streptococcus mutants.
    Author: Hu GJ, Li LF, Li D, Liu C, Wei SC, Liang YH, Su XD.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2007 Sep 01; 63(Pt 9):809-11. PubMed ID: 17768362.
    Abstract:
    The SMU.636 protein from Streptococcus mutans is a putative glucosamine 6-phosphate deaminase with 233 residues. The smu.636 gene was PCR-amplified from S. mutans genomic DNA and cloned into the expression vector pET-28a(+). The resultant His-tagged fusion protein was expressed in Escherichia coli and purified to homogeneity in two steps. Crystals of the fusion protein were obtained by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.4 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.83, b = 82.13, c = 134.70 A.
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