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...
| Autores principales: | , , , , |
|---|---|
| Formato: | Journal article |
| Lenguaje: | English |
| Publicado: |
2008
|