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. Author manuscript; available in PMC: 2012 Oct 1.

Published in final edited form as: Bioorg Med Chem. 2011 Aug 16;19(19):5886–5895. doi: 10.1016/j.bmc.2011.08.012

Fig. 5 — (a) Purification of recombinant Y. pestis CDP-ME kinase by Nickel-affinity chromatography. Comassie blue-stained SDS-PAGE showing cell lysate from E. coli bacterial cells over-expressing Y. pestis CDP-ME kinase.

(b) Amino acid sequence alignment of CDP-ME kinases from E. coli, Shigella dysenteriae, Salmonella typhi, and Y. pestis. Residues highlighted in red are identical residues across all four species and residues highlighted in blue are conserved residues.

Fig. 5 — (a) Purification of recombinant Y. pestis CDP-ME kinase by Nickel-affinity chromatography. Comassie blue-stained SDS-PAGE showing cell lysate from E. coli bacterial cells over-expressing Y. pestis CDP-ME kinase.

(b) Amino acid sequence alignment of CDP-ME kinases from E. coli, Shigella dysenteriae, Salmonella typhi, and Y. pestis. Residues highlighted in red are identical residues across all four species and residues highlighted in blue are conserved residues.