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Title: Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer
Authors: Ren, J
Nettleship, JE
Sainsbury, S
Saunders, NJ
Owens, RJ
Keywords: Cold-shock domain proteins;Neisseria meningitidis;Domain-exchanged dimers
Issue Date: 2008
Publisher: International Union of Crystallography
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 4): 247 - 251, Apr 2008
Abstract: 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 -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.
Description: Copyright @ 2008 International Union of Crystallography
ISSN: 1744-3091
Appears in Collections:Biological Sciences
Dept of Life Sciences Research Papers

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