I am very grateful to Queen Mary, University of London, for contracting me to an academic faculty position (2012-), taking on a "Principal Research Fellow"-role (0.69 FTE) within The School of Biological and Chemical Sciences. 1. I was an independent University Research Fellow of The Royal Society position (2001-2012; at Imperial College London, until 2007). The Royal Society University Research Fellowship (£273,040 + £386,464 + £194,000; extended to 30/09/2012); with additional funding being awarded through the UK Government's Biotechnology and Biological Sciences Research Council (BBSRC; see below), The Royal Society grants schemes and The Biochemical Society travel awards (various £k amounts).
2. The lab was engaged in projects with Japan under the JST/CREST initiative "Structural characterisation of the transient macromolecular complexes engaged in photoacclimation" (2013-2019; grant number JPMJCR13M4) - consortium budget ~2.0-2.5m GBP; five overseas visits, including Special Advisor to Osaka University (2015). 3. The London Consortium for Electron Microscopy (LonCEM) was awarded a major grant by The Wellcome Trust (~3m GBP, March 2017), the lab being a named group within the QMUL partner's contribution, reinforced by an additional BBSRC grant for a new cryo-TEM facility (April 2017). 4. Support from the BBSRC (UK research council; c/f their OASIS database):
Grant Reference: BB/M023877/1 Title: Fundamental membrane interactions of copper generated oligomers, profibrils and amyloid fibres Institution of Grant: Queen Mary, University of London PI, Viles J; co-PIs, Nield J (with Mark Baker, Lilia Milanesi and Matteo Palma) Edited Abstract: There are a range of diseases including Mad-cow and Alzheimer's disease (AD) whose etiology involves proteins that self-associate into oligomers and amyloid fibers. It is this misassembly, of amyloid beta peptide (Ab), in the case of Alzheimer's disease, culminates in cell-death and dementia. Ab is a small peptide 40 or 42 amino acids long and there is strong evidence that oligomers of Ab42, but not Ab40, are the most cytotoxic. The effect of Cu-Ab-oligomers on liposome models of the bi-layer will facilitate the first 3D structures of lipid membrane disruption by oligomers. End date: 31/05/19, Duration: 46 months Total Value of Grant: £346,238 Grant Reference: BB/R000514/1 Title: A cryo-electron microscope for structural and cell biology Institution of Grant: Queen Mary, University of London PI, Pickersgill, R; co-PIs, Nield J, and Vidya Chandran Darbari, Viji Draviam, James Garnett, Ewan Main, Lilia Milanesi, Conrad Mullineaux, Maxie Roessler, Alexander Ruban, Benjamin Stieglitz, John Viles Edited Abstract: Advances in detector technology and image analysis algorithms have made cryo-EM the structural method of choice for large macromolecular complexes especially those with intrinsic dynamic properties and those available in only small quantities. With cryo-EM 100-1000 times lower protein concentration may be used as compared to X-ray crystallography one does not have to lock complexes into a single conformation. Each particle is imaged individually and may be sorted in silico according to their conformation, with research extended using cryo-tomography. End date: 07/08/18, Duration: 12 months Total Value of Grant: £302,000
Grant Reference: BBF0215261 Title: Molecular basis of FtsH function in the cyanobacterium Synechocystis PCC 6803 Institution of Grant: Queen Mary, University of London PI, Nield J Edited Abstract: FtsH proteases, which are members of the AAA+ (for ATPase associated with various cellular activities) superfamily of proteins, play an important physiological role in the cyanobacterium, Synechocystis 6803, including the acclimation to various type of abiotic stress (e.g., light, heat and salt stress). A wide-ranging investigation into the structure and function of the four FtsH homologues found in Synechocystis 6803 will be conducted. End date was: 29/05/12, Duration: 39 months Total Value of Grant: £28,883 BB/D524840/1 Title: A high-throughput crystallisation facility for protein structure determination Institution of Grant: Imperial College London PI, Hohenester, E; co-PIs, Nield J, and Geoffrey Baldwin, James Barber, Peter Brick, Katherine Brown, Martin Buck, Elisabeth Carpenter, Naomi Chayen, Stephen Curry, Paul Freemont, So Iwata, Stephen Matthews, Silvia Onesti, Robert Weinzierl, Xiaodong Zhang Conclusions: This application provided for a robotic nanolitre protein crystallisation facility for the Centre for Structural Biology (CSB) at Imperial College London. The CSB is a college centre with affiliated groups from three faculties and provides both expertise and managed core facilities in all major techniques of macromolecular structure determination: X-ray crystallography, nuclear magnetic resonance spectroscopy, and electron microscopy. Robotic crystallisation has become essential to make progress in the emerging area of system-wide structural biology. End date was: 23/02/07, Duration: 9 months Total Value of Grant: £188,124
Grant Reference: B17532 Title: Using C. reinhardtii as a model system for determining the macromolecular structure of PSI and PSII by high resolution electron microscopy Institution of Grant: Imperial College London PI, Nield J; co-PI, Barber J Conclusions: The transformable green alga, C. reinhardtii, was used as a model system to obtain structural information about the macromolecular organisation of photosystem I (PSI) and photosystem II (PSII), in higher plants and other photosynthetic eukaryotic organisms that contain chlorophyll a/b light harvesting complexes (LHC) using electron cryo-microscopy and single particle analysis. Related studies were conducted to isolate and characterise a novel LHCI-PSI supercomplex, by negative stain electron microscopy (EM). End date was: 1/01/06, Duration: 36 months Total Value of Grant: £203,160
Grant Reference: C11886 Title: Elucidating the structure of photosystem two by cryoelectron microscopy and single particle analyses Institution of grant: Imperial College London PI: Barber J; co-PIs Nield J and Van Heel M Conclusions: This programme obtained a 3D structure of photosystem II (PSII) from spinach at 1.7 nm resolution using cryo-electron microscopy and single particle analyses. In addition, a 3D structure of the LHCII-PSII supercomplex from C. reinhardtii was determined. All structures obtained were analysed in order to highlight similarities and differences with their 3D maps used as frameworks for incorporating structures of various subunits and subcomplexes obtained from X-ray and electron crystallography. Start date: 16/10/99; left project upon award of Royal Society Fellowship 01/10/01 Total Value of Grant: £204,841
Grant Reference: C06795 Title: Structure determination of a multi-subunit supercomplex of photosystem II by single particle analysis of cryo-electron micrographs Institution of grant: Imperial College London PI: Barber J; co-PI: Van Heel M Post-doctoral researcher: Nield J Conclusions: New and powerful techniques in the image processing of single particles from cryo-electron microscopy were used to reconstruct a 3D map of the multi-subunit supercomplex, photosystem II. This map was used to determine the position of subunits of this protein complex in order to understand the structural information obtained in the context of energy transfer, charge separation and water splitting. Start date: 1/01/97 End date was: 30/09/99 Total Value of Grant: £173,054
Journals I acknowledge and thank the editorial teams and scientific referees of all the Journals that have published details of my co-authored research.
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