Organisation of Outer membrane protein F at the air/liquid interface

DOI

Crystallisation of membrane proteins as a precursor to high resolution structural studies is a significant research bottleneck. We are investigating alternative methods to achieve low to medium resolution structural studies. One approach we are investigating involves spreading at the air/liquid interface OmpF from vesicles to form stable Langmuir films which can then be manipulated using standard surface methods and deposited as ordered monolayers onto solid substrates. We have promising data from the first stage of this process, that is, films at the air liquid interface. Using a range of contrast variation this proposal will enable characterisation of the dimensions and relative proportions of subphase, lipid and protein in the layer.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24068752
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24068752
Provenance
Creator Dr Stephen Holt; Dr Luke Clifton; Professor Jeremy Lakey; Dr Mario Campana
Publisher ISIS Neutron and Muon Source
Publication Year 2012
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 2009-06-06T09:41:23Z
Temporal Coverage End 2009-06-10T10:32:49Z