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


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.

SUBMITTER: Zhou YF 

PROVIDER: S-EPMC2373987 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature

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

Zhou Yan-Feng YF   Li Lan-Fen LF   Yang Cheng C   Liang Yu-He YH   Su Xiao-Dong XD  

Acta crystallographica. Section F, Structural biology and crystallization communications 20071220 Pt 1


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  ...[more]

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