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Updated: Jul 9, 2026
Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans
Yan-Feng Zhou1, Lan-Fen Li, Cheng Yang
1National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Abstract:
SMU.573 from Streptococcus mutans is a structurally and functionally uncharacterized protein that was selected for structural biology studies. Native and SeMet-labelled proteins were expressed with an N-His tag in Escherichia coli BL21 (DE3) and purified by Ni2+-chelating and size-exclusion chromatography. Crystals of the SeMet-labelled protein were obtained by the hanging-drop vapour-diffusion method and a 2.5 A resolution diffraction data set was collected using an in-house chromium radiation source. The crystals belong to space group I4, with unit-cell parameters a = b = 96.53, c = 56.26 A, alpha = beta = gamma = 90 degrees.
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