Jon
has received funding from the UK governement BBSRC (Biotechnology
and Biological Sciences Research Council), The Wellcome Trust, The Leverhulme
Trust and
Japan's Science and Technology Agency (2014-2019). He
remains very appreciative that his work was recognised
and supported by The
Royal Society - "Investigating photosynthetic
complexes by single particle analysis (11 yrs) " - and
various grants from the UK's BBSRC
Research Council (see below).
Full
funding list:
5. Principal
Research Fellow-role (0.69 FTE) within The
School of Biological and Chemical Sciences at Queen
Mary, University of London, (2012-2020).
4. I held 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 from the BBSRC, The Royal
Society grants schemes and The Biochemical Society
travel awards.
3. Recently, the lab has been engaged in projects
with Japan under their JST/CREST initiative
"Structural characterisation of the transient
macromolecular complexes engaged in
photoacclimation" (2013-2019, PI: Kurisu, G., grant
number JPMJCR13M4) - total consortium budget
~2.0-2.5m GBP, of which ~225-250k GBP awarded to
Foreign PI: Nield.
2. The London
Consortium for Electron Microscopy (LonCEM)
has been 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 a BBSRC grant for a new cryo-TEM facility at QMUL
(2018-, Grant Reference: BB/R000514/1, see below).
1. I have
contributed to the following BBSRC grants (from
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 all the Journals that
have published details of my co-authored research.
Content
Website design & implementation by Jon Nield.
Photo
credits: My own work (see EXIF data), unless
specifically noted in the webpage footer or on the
image itself.
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