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The structure of the cold‐shock domain protein from Neisseria meningitidis has been solved to 2.6 Å resolution and shown to comprise a dimer formed by the exchange of two β‐strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold‐shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a Kd of 1.25 µM.
Acta Crystallographica Section F – Wiley
Published: Apr 1, 2008
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