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Updated: Jun 17, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Preliminary crystallographic studies of purine nucleoside phosphorylase from the cariogenic pathogen Streptococcus
Qiao Ming Hou1, Xiang Liu, Erik Brostromer
1Peking University Shenzhen Graduate School, Shenzhen 518055, People's Republic of China.
Abstract:
The punA gene of the cariogenic pathogen Streptococcus mutans encodes purine nucleoside phosphorylase (PNP), which is a pivotal enzyme in the nucleotide-salvage pathway, catalyzing the phosphorolysis of purine nucleosides to generate purine bases and alpha-ribose 1-phosphate. In the present work, the PNP protein was expressed in Escherichia coli strain BL21 (DE3) in a soluble form at a high level. After purification of the PNP enzyme, the protein was crystallized using the sitting-drop vapour-diffusion technique; the crystals diffracted to 1.6 A resolution at best. The crystals belonged to space group H3, with unit-cell parameters a = b = 113.0, c = 60.1 A.

