Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.
The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock prot...
| Hlavní autoři: | , , , , |
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| Médium: | Journal article |
| Jazyk: | English |
| Vydáno: |
2008
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