The CF-1 cell disruptor has been key to our research within the Pliotas laboratory at the University of Manchester. This system allows for rapid and consistent cell lysis of our bacterial, yeast, and human samples, ensuring prep-to-prep reproducibility of diverse membrane protein preparations for structural and functional characterisation. The CF-1 is very easy to use, which makes training new members of staff straightforward. Additionally, the ability to easily clean and maintain the system using the clean-in-place protocols set out during installation allows for quick transitions between different protein purification samples.
Further, the CF-1’s ability to cool samples during the cell disruption process means that we are able to maintain the correct conformation of our membrane proteins for high resolution structural and EPR spectroscopy studies. Overall, we believe that the CF-1 has been instrumental in progressing our research as highlighted by a number of publications from the laboratory where the CF-1 played a key role in purification.
Christos Pliotas – FRSB, Dr
Reader in Structural Biological EPR Spectroscopy, Division of Molecular & Cellular Function (L5)
Structural basis of the gating mechanism of the large-conductance mechanosensitive channel from Escherichia coli
Publication list (*denotes corresponding author)
1. Hardman, K., Wort, J.L., Waheed, Q., Liu, X., Arul, D., Porav, S.A., Calabrese, A.N., Muench S.P., Pliotas*, C. (2026) Structural basis of the gating mechanism of the large-conductance mechanosensitive channel from Escherichia coli. Nature Communications (DOI: 10.1038/s41467-026-76193-0) (in press)
2. Ma, Y., Ackerman, K., Waheed, Q., Postis, V., Smith T.K., Bode B.E., Pliotas*, C. (2026) Swapped and non-swapped TRAAK states co-exist in membranes at a ratio influenced by temperature. Nature Communications (https://www.nature.com/articles/s41467-026-70027-9)
3. Ettema, T., Inaba-Inoue, S., Thangaratnarajah, C., Da Silva, L.A., Clarke, A., Stepien, P., Shah, A., Ma, Y., Hardman, K., David, S., El-Mkami, H., Heddle, J., Nomura, N., Ogasawara, S., Iwata, S., Ghilarov*, D., Pliotas*, C., Stockner*, T., Slotboom*, D., Beis*, K. (2026) Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters. Nature Communications (https://www.nature.com/articles/s41467-026-71633-3)
4. Lane, B.J., Dionysopoulou, M., Yan, N., Lippiat, J.D., Muench, S.P., Pliotas*, C. (2025) The mechanosensitive channel YbiO has a conductance equivalent to the largest gated-pore. Structure 33: 1-11 (doi: 10.1016/j.str.2025.01.014)
5. Liu, J., Shah, A., Ma, Y., Hardman, K., Johansson, N.J., Ribeiro, O., Brookfield, A., Bowen, A., Yli-Kauhaluoma, Y., Xhaard, H., Jeuken, L.J.C., Goldman*, A., Pliotas*, C., Vidilaseris*, K. (2025) Conformational dynamics and asymmetry in multimodal inhibition of membrane-bound pyrophosphatases. eLife (doi: 10.7554/eLife.102288.1)
6. Lane, B.J., Ma, Y., Yan, N., Wang, B., Ackermann, K., Karamanos, T.K., Bode, B.E., Pliotas*, C. (2024) Monitoring the Conformational Ensemble and Lipid Environment of a
Mechanosensitive Channel Under Cyclodextrin-Induced Membrane Tension. Structure 32: 1-12 (doi:10.1016/j.str.2024.02.020)
7. Haysom, S.F., Machin, J., Whitehouse, J.M., Horne, J.E., Fenn, K., Ma, Y., Hassane El Mkami, Nils Böhringer, Schäberle, T.F., Ranson, N.A., Radford*, S.E., Pliotas*, C. (2023) Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells. Angewandte Chemie International Edition, p.e202218783 (doi: 10.1002/ange.202218783)
