Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae

Authors: Riboldi-Tunnicliffe, Alan; Bent, Colin J.; Isaacs, Neil W.; Mitchell, Timothy J.

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 926-928(3)

Publisher: Blackwell Publishing

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Abstract:

A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 Å, β = 90.01°. The crystals diffract X-rays to beyond 1.2 Å resolution.

Keywords: Streptococcus pneumoniae; pneumococcal histidine triad protein A; PhtA; structural genomics

Document Type: Research article

DOI: 10.1107/S0907444904004573

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