Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 9 (September 2007)

crystallization communications

Acta Cryst. (2007). F63, 809-811 [ doi:10.1107/S1744309107040304 ]

Protein preparation and preliminary X-ray crystallographic analysis of a putative glucosamine 6-phosphate deaminase from Streptococcus mutants

G.-J. Hu, L.-F. Li, D. Li, C. Liu, S.-C. Wei, Y.-H. Liang and X.-D. Su

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 Å resolution and belong to space group P2₁2₁2₁, with unit-cell parameters a = 53.83, b = 82.13, c = 134.70 Å.

Keywords: SMU.636; Streptococcus mutans; glucosamine 6-phosphate deaminase.