ISIS Neutron and Muon Source Data Journal

The solution structure of E.coli peripheral membrane protein FtsA solubilised within a polymer stabilised nanodisc

Abstract: We will measure the solution structure of a protein complex from bacteria essential for cell division. The two proteins, FtsA and FtsZ, are known to interact with each other with FtsZ forming a constricting ring, and FtsA being a membrane protein anchoring this ring to the membrane. Furthermore, we have prepared these proteins in a novel way using SMALPs: discoidal structures solubilising membrane proteins within a native lipid environment without the use of detergents which are a poor substitute for the natural lipid bilayer. While interactions are known, the structural details of the assembly are unknown. We propose to use small angle neutron scattering on SANS2D to measure the solution structure of this complex isolated in the most native-like state by using SMALPs, which is essential for the development of novel antibiotics and understanding the mechanism of bacterial cell division.

Principal Investigator: Dr Thomas Arnold
Experimenter: Professor Karen Edler
Experimenter: Dr Stephen Hall
Local Contact: Dr Najet Mahmoudi
Experimenter: Dr Andrew McCluskey
Experimenter: Dr Luke Clifton
Experimenter: Dr Tim Knowles
Experimenter: Dr Ian Cadby
Experimenter: Dr Mark Jeeves

DOI: 10.5286/ISIS.E.RB1710049

ISIS Experiment Number: RB1710049

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Thomas Arnold et al; (2017): The solution structure of E.coli peripheral membrane protein FtsA solubilised within a polymer stabilised nanodisc, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1710049

Data is released under the CC-BY-4.0 license.