About the Project
Life on earth depends on photosynthesis, which converts sunlight into chemical energy via coupled electron-proton transfer reactions in the chloroplast. These life-giving reactions depend on complex conformational dynamics of the proteins involved. However, the structural details underlying these dynamics have largely remained invisible to cryo-electron microscopy (cryo-EM) due to ensemble averaging effects. This limitation has recently been overcome by development of three-dimensional variability (3DVA) analysis, which resolves structural heterogeneity. The challenge is now to harness these methods to obtain a complete understanding of structure and function relationships in photosynthetic proteins.
This project will investigate the molecular structures and conformational movements involved in the coupling between electron and proton transfer in these complexes. The ongoing “resolution revolution” of cryo-EM makes it an ideal technique for assessing these large supramolecular complexes at the single-particle level.
The successful candidate will gain experience from experts in the field of molecular genetics, biochemistry, biophysics and proteomics within the large Photosynthesis Research Group at Sheffield (www.sheffield.ac.uk/photosynthesis) and structural biology at the National Cryo Electron Microscopy Facility at Diamond in Oxford (https://www.diamond.ac.uk/Instruments/Biological-Cryo-Imaging/eBIC.html).
For more information please see: https://www.sheffield.ac.uk/photosynthesis/phd-studentship-opportunity
About the DTP
This studentship is offered as part of the White Rose BBSRC Doctoral Training Partnership (DTP) in Mechanistic Biology, which brings together the research of the world-class molecular and cellular bioscience centres at the White Rose universities of Leeds, Sheffield and York.
Our mission is to train excellent bio-scientists who understand how living systems work
and can innovate to address global challenges, such as the impact of climate change, a healthier old age, sustainable food production, land use and energy production.
What is on offer?
This is a core/iCASE studentships for entry in October 2024.
Join us and you will receive a 4-year, funded PhD programme of research and skills training, with cross-disciplinary supervision, plus a structured programme of cohort-wide training and networking events. A highlight is the annual symposium, which is planned and delivered by students.
A unique part of your training will be the Professional Internships for PhD Students (PIPS), where you will spend three months at a host organisation of your choosing, gaining experience of work in a professional environment, and acquiring transferable skills that will be beneficial in your future career.
How to apply – Expression of Interest
Students may apply for up to three projects anywhere in the Doctoral Training Partnership (DTP). Applications will be to the DTP centrally, using an online Expression of Interest (EoI). The EoI will include:
§ CV information; not submitted separately
§ Equality, Diversity and Inclusion (EDI) data
§ Names of two referees
Deadline for EoIs is midnight Sunday 7th January 2024.
Submit EoIs using this link: https://leeds.onlinesurveys.ac.uk/white-rose-bbsrc-dtp-expression-of-interest-form
Shortlisted candidates will be required to make formal applications to the Graduate School at each institution, supplying the necessary paperwork.
Interviews will be held either Friday 2nd and Monday 5th to Friday 9th February, or Monday 19th to Friday 23rd and Monday 26th February 2024, in-person at Leeds, Sheffield and York, with a panel representing all 3 Universities. Shortlisted candidates will be notified of a specific time/date to attend. If you have applied for more than one project and are selected for interview, you will be interviewed only once.
Proctor M, Malone L, Farmer D, Swainsbury D, Hawkings F, Pastorelli F, Emrich-Mills TZ, ,Siebert CA, Hunter CN, Johnson MP, Hitchcock A (2022) Cryo-EM structures of the Synechocystis sp. PCC 6803 cytochrome b6f complex with and without the regulatory PetP subunit. Biochem J. 479, 1487–1503.
Hepworth C, Wood WHJ, Emrich-Mills TZ, Proctor M, Casson S, Johnson MP (2021) Dynamic thylakoid stacking and state transitions work synergistically to avoid acceptor-side limitation of photosystem I. Nature Plants. 7, 87-98.
Malone L, Qian P, Mayneord G, Hitchcock A, Farmer DA, Thompson RF, Swainsbury DK, Ranson NA, Hunter CN, Johnson MP (2019) Cryo-EM structure of the spinach cytochrome b6f complex at 3.6Å resolution. Nature. 575, 535-539.
MacGregor-Chatwin C, Nurnberg DJ, Jackson PJ, Vasilev C, Hitchcock A, Ho MY, Shen G, Gisriel CJ, Wood WHJ, Mahbub M, Selinger VM, Johnson MP, Dickman MJ, Bryant DA, Rutherford WA, Hunter CN (2021) Changes in supramolecular organisation of cyanobacterial thylakoid membrane complexes in response to far-red light photoacclimation. Science Advances. 8, eabj4437.
Swainsbury, D.J.K., Hawkings, F.R., Martin, E.C., Musial, S., Salisbury, J.H., Jackson, P.J., Farmer, D.A., Johnson, M.P., Siebert, C.A., Hitchcock, A. and Hunter, C.N. (2023) Cryo-EM structure of the four-subunit Rhodobacter sphaeroides cytochrome bc1 complex in styrene maleic acid nanodiscs. Proc. Natl. Acad. Sci. U. S. A. 120(11), e2217922120. https://doi.org/10.1073/pnas.2217922120.
Proctor, M.S., Malone, L.A., Farmer, D.A., Swainsbury, D.J.K., Hawkings, F.R., Pastorelli, F., Emrich-Mills, T.Z., Siebert, C.A., Hunter, C.N., Johnson, M.P. and Hitchcock, A. (2022) Cryo-EM structures of the Synechocystis sp. PCC 6803 cytochrome b6f complex with and without the regulatory PetP subunit. Biochem. J. 479(13), 1487-1503. https://doi.org/10.1042/BCJ20220124.
Qian, P., Croll, T.I., Hitchcock, A., Jackson, P.J., Salisbury, J.H., Castro-Hartmann, P., Sader, K. Swainsbury, D.J.K., and Hunter, C.N. (2021) Cryo-EM structure of the dimeric Rhodobacter sphaeroides RC-LH1 core complex at 2.9 Å: the structural basis for dimerisation. Biochem. J. 478(21), 3923-3937. https://doi.org/10.1042/BCJ20210696.
Swainsbury, D.J.K., Qian, P., Jackson, P.J., Faries, K.M., Niedzwiedzki, D.M., Martin, E.C., Farmer, D.A., Malone, L.A., Thompson, R.F., Ranson, N.A., Canniffe, D.P., Dickman, M.J., Holten, D., Kirmaier, C., Hitchcock, A. and Hunter, C.N. (2021) Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels. Sci. Adv. 7(3), eabe2631. https://doi.org/10.1126/sciadv.abe2631.