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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 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 protein...
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| Asıl Yazarlar: | , , , , |
|---|---|
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
International Union of Crystallography
2008
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2374261/ https://ncbi.nlm.nih.gov/pubmed/18391418 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309108005411 |
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