Brunel University Research Archive(BURA) preserves and enables easy and open access to all
types of digital content. It showcases Brunel's research outputs.
Research contained within BURA is open access, although some publications may be subject
to publisher imposed embargoes. All awarded PhD theses are also archived on BURA.
Please use this identifier to cite or link to this item:
http://bura.brunel.ac.uk/handle/2438/6647Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Ren, J | - |
| dc.contributor.author | Nettleship, JE | - |
| dc.contributor.author | Sainsbury, S | - |
| dc.contributor.author | Saunders, NJ | - |
| dc.contributor.author | Owens, RJ | - |
| dc.date.accessioned | 2012-09-14T12:30:23Z | - |
| dc.date.available | 2012-09-14T12:30:23Z | - |
| dc.date.issued | 2008 | - |
| dc.identifier.citation | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(Pt 4): 247 - 251, Apr 2008 | en_US |
| dc.identifier.issn | 1744-3091 | - |
| dc.identifier.uri | http://onlinelibrary.wiley.com/doi/10.1107/S1744309108005411/abstract | en |
| dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/6647 | - |
| dc.description | Copyright @ 2008 International Union of Crystallography | en_US |
| dc.description.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. | en_US |
| dc.description.sponsorship | This study is funded by the UK Medical Research Council. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | International Union of Crystallography | en_US |
| dc.subject | Cold-shock domain proteins | en_US |
| dc.subject | Neisseria meningitidis | en_US |
| dc.subject | Domain-exchanged dimers | en_US |
| dc.title | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer | en_US |
| dc.type | Article | en_US |
| dc.identifier.doi | http://dx.doi.org/10.1107/S1744309108005411 | - |
| pubs.organisational-data | /Brunel | - |
| pubs.organisational-data | /Brunel/Brunel Active Staff | - |
| pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care | - |
| pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care/Biological Sciences | - |
| pubs.organisational-data | /Brunel/Group Publication Pages | - |
| pubs.organisational-data | /Brunel/University Research Centres and Groups | - |
| pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups | - |
| pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups/Centre for Systems and Synthetic Biology | - |
| Appears in Collections: | Biological Sciences Publications Dept of Life Sciences Research Papers | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Fulltext.pdf | 594.99 kB | Adobe PDF | View/Open |
Items in BURA are protected by copyright, with all rights reserved, unless otherwise indicated.