Determining the structure of the colicin OmpF complex

DOI

Large multiprotein complexes are the new frontier in structural biology. Individual proteins may be solved by X-ray crystallography but the relationships between subunits and their adopted conformations are accessible to SANS studies. We are studying a complex that is not only important for the biology of E.coli bacteria but also represents many membrane bound complexes across biology. The protein colicin N uses the receptor OmpF to translocate across the outer membrane and kill the cell. Using combinations of deuterated protein, detergent and water we are able to separate the components of the complex and resolve their interactions. We wish to use SANS 2D to obtain a wide range of Q in order to model the structure in detail. Initial data has confirmed stability of the samples and the benefits of aqueous phase contrast variation.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24086447
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24086447
Provenance
Creator Dr Stephen Holt; Professor Jeremy Lakey; Ms Nat Arunmanee; Dr Chris Johnson
Publisher ISIS Neutron and Muon Source
Publication Year 2014
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2011-07-30T08:16:01Z
Temporal Coverage End 2011-07-31T15:04:48Z