I was awarded a Royal Society University Fellowship “Investigating Photosynthetic Complexes” in late 2001. This was, gratefully, extended to 2012 due to medical circumstances (I have been 0.5/0.65 FTE since 2008). My Fellowship’s central remit was to probe more evolutionarily diverse organisms and mutants for light-harvesting photosynthetic proteins, and to drive forward a combinatorial approach of TEM and computer purification to overcome the structural heterogeneity often observed in light-sensitive samples. This resulted in an output of over 25 primary papers, and, further to this, separate structural breakthroughs were made for proteins involved in bacterial pathogenesis (PspA) and for antibiotic resistance (emrAB complex). Photosystem assembly (Ycf4 protein; ref: The Plant Cell, 2009) and red algal light harvesting (Lhcr proteins) were also reported upon. X-ray diffraction was used to probe a cyanobacterial light-harvesting protein, subsequently elucidated to a resolution of 1.45 Å in 2003 (the most highly resolved light harvesting protein at that time (for two years; with diffraction spots out to 1.1 Å). Other projects used Atomic Force Microscopy to investigate molecular dynamics within membranes. I have contributed to/designed/awarded 11 front covers of books and journals.
During the earliest stages of my career (summer 1993), I was fortunate to isolate and fully characterise the first ever membrane-bound “photosynthetic supercomplex” (ref: PNAS, 1995) whilst working in the superb, vibrant, laboratory of Professor James Barber at Imperial College London, together with Dr. Ben Hankamer (now Professor at the University of Queensland, Australia) and in collaboration with Professor Egbert Boekema (Groningen) and Professor Matthias Roegner (Bochum). This has opened up a large field of international investigation surrounding photosystem/light-harvesting supercomplexes. At that time, for my Ph.D. studies, I probed this (relatively huge, 33 nm diameter, elongated >1.2 megaDalton) PSII-LHCII supercomplex using 14 biochemical/biophysical techniques, gaining a Ph.D. in 1997, then followed this by its structural elucidation to 17 Å via cryo-TEM during two post-doctoral positions (refs: Nature/Nature Structural Biology). The use at that time of (relatively novel) vitrified samples permitted 3D structures to be calculated from a number of organisms (cyanobacteria, green algae and a diverse range of niche organisms and their mutants) by cryo-TEM and single particle image analysis (17-20 Å resolution). It is most satisfying to see the Nobel Prize for Chemistry (2017) being awarded to 3 incredible scientists who have played such an intrinsic role in bringing the field of cryo-EM into the state it is in, today. Indeed, it is the review paper of Dr. Henderson (Quart. Rev. Biophys. 1995) that played a big part of my thinking during my thesis write-up, and in fact the motivation to apply for a PDRA position with Professor Marin van Heel in 1997, and visits of mine to the LMB in Cambridge in the late 1990's … that provided me with such impetus to achieve my early career contributions.
The lab engages in many national/international collaborations with emphasis now on the mechanisms and complexes that assemble, repair and regulate these membrane proteins in the first instance, including the first 3D reconstruction of the PSII-affecting protease FtsH (ref: The Plant Cell, 2012). Visiting researchers and/or Ph.D. students are welcome to contact the lab. I aid the revision of the IBID Press (Biology) textbooks (Hodder, ed. C. Talbot) as a consultant, for the International Baccalaureate (2014-present).
I referee publications for many journals, both specialist and well known, and grants for the scientific community. I was an Associate Editor of Photochemical & Photobiological Sciences (01/2005 to 12/2009; www.rsc.org/pps). I have been, concurrently, Staff Representative on Faculty and GM-safety committees, as well as organising a seminar series (26 lectures in 18 months), while sitting on Departmental IT provision committees. For the past five years, these skills have turned to being the Careers Liaison Officer for my School's (Department's) biology-degree students (800+ individuals) and a management committee member for QMUL's NanoVision TEM/SEM Centre (on the Mile End campus, E1 4NS, London, UK).
Funding has been gratefully received over the years from The Royal Society, the BBSRC/UK government, The Biochemical Society and Japan's JST/CREST initiative, amongst others.
All original scientific content within this website is copyright of myself, the relevant authors, institutions and/or the journals that it is published in, as indicated.