I’m very excited to share the first big project from my PhD (my first proper-first, yay!) where we use cryoET and a fun new flavour of CLEM to study the re-organisation of photosynthetic machinery of cyanobacteria growing beyond the red limit of light. doi.org/10.64898/202...

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The STA structures show that the geometry of the supercomplex is different in FRL (red) than in WL (blue)-- or any other structure for that matter. This positions the PBS directly over the most efficient energy transfer path in PSII, explaining why far-red photosynthesis is so remarkably efficient.

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Because we can see individual protein complexes with cryoET, we were able to see a very small population of PBS that were not forming rows as we would expect: turns out they are part of a different complex altogether: in FRL, we find a unique PBS-PSI supercomplex.

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We put these cyanobacteria under the magnifying glass to see how they completely re-organise their photosynthetic machinery to maintain efficient photosynthesis in far-red light. With cryoET and subtomogram averaging, we show how the antenna-photosystem complex is remodelled at the molecular level.

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Check out an epic new study by star student Matt Howard 🤩!!! We've been working on this for many years and we generate a ridiculous amount of data to address a classic gpcr question using the opioid receptor as a model - how do ligands binding to the same site activate receptors to varying degrees!

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