Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans

1Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.
Get full text

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 Å 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 Å, α = β = γ = 90°. © International Union of Crystallography 2008.

Author supplied keywords

Cite

CITATION STYLE

APA

Zhou, Y. F., Li, L. F., Yang, C., Liang, Y. H., & Su, X. D. (2008). Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(1), 47–49. https://doi.org/10.1107/S1744309107065645

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free