[3dem] Postdoc available in Bristol (UK) in high resolution electron microscopy data processing

Ariel Blocker Ariel.Blocker at bristol.ac.uk
Thu Mar 9 03:59:58 PST 2017

The closing date for applications is midnight Sunday 26 March 2017

Further particulars available at
http://www.bristol.ac.uk/jobs/find/details.html?nPostingId=5607&nPostingTargetId=21269&id=Q50FK026203F3VBQBV7V77V83&LG=UK&mask=uobext <http://www.bristol.ac.uk/jobs/find/details.html?nPostingId=5607&nPostingTargetId=21269&id=Q50FK026203F3VBQBV7V77V83&LG=UK&mask=uobext>

We seek an enthusiastic Research Associate specialised in high resolution electron microscopy data processing to join the team of Dr. Ariel Blocker on a project funded by a 4-year Wellcome Trust Investigator Award to Dr. Ariel Blocker entitled “Molecular mechanisms powering a bacterial injection device”.
Type III secretion systems (T3SSs) are essential devices in the virulence of many Gram-negative bacterial pathogens. They translocate bacterial virulence proteins into eukaryotic host cells to manipulate them during infection [1]. T3SSs involved in virulence (vT3SSs) are evolutionarily related to bacterial flagella assembly apparatuses (fT3SSs) [2]. The central function of T3SSs, the translocation process, is energised solely by the cytoplasmic and inner membrane export apparatus (CIMEA), which mediates the passage of substrates across the bacterial inner membrane. The cytoplasmic export apparatus (CEA) comprises an ATPase complex attached to the inner membrane T3SS base. The inner membrane export apparatus (IMEA) probably forms the export pore inside the T3SS base. But, the architecture of the cytoplasmic and inner-membrane export apparatus is not well defined and how energy from ATP hydrolysis and the proton motive force is utilised to drive substrate export remains obscure. To investigate this, we focus on the IMEA and how it interfaces with the CEA. We work on two well-understood T3SSs, the Shigella vT3SS and the Salmonella fT3SS.

The Research Associate will collaborate tightly with two PhD students midway through their theses who are overexpressing and purifying the fT3SS IMEA for electron microscopy and single particle analysis and investigating the architecture of the vT3SS [3] in different states of secretion by cryo electron tomography.

The post is funded for 22 to 24 months and will be held primarily within the School of Cellular and Molecular Medicine in Bristol.

For further information on the research group please visit: http://www.bris.ac.uk/cellmolmed/staff/blocker.html <http://www.bris.ac.uk/cellmolmed/staff/blocker.html>. For details of the current Bristol electron microscopy facilities, please visit: http://www.bristol.ac.uk/biochemistry/wbif <http://www.bristol.ac.uk/biochemistry/wbif>.  In the first half of 2017, the new South-West Regional Facility for High-Resolution Cryo-EM, funded by the Wellcome Trust, will become operational at the University of Bristol, outfitted with a FEI Talos Arctica cryo-microscope, energy filter and a Gatan K2 Summit direct electron detector. It will also serve as a feeder instrument into the BBSRC-funded National Facility for Electron Cryo-Microscopy at Harwell (eBIC) with currently two Titan Krios cryo-microscopes. Funds are currently being sought to establish in addition a high-performance computing resource for cryo-EM image processing at University of Bristol. This HPC cluster (BlueCryo) will be maintained and manage by a dedicated Systems Administrator supported by the Advanced Computing Research Centre at Bristol and fully accessible to the person we hire.

Informal enquiries would be welcome to: Dr. A. Blocker (ariel.blocker at bristol.ac.uk) <mailto:ariel.blocker at bristol.ac.uk)>.


[1] Cheung, M et al. Three-dimensional electron microscopy reconstruction and cysteine-mediated crosslinking provide a model of the T3SS needle tip complex. <http://www.ncbi.nlm.nih.gov/pubmed/25353930> Mol Microbiol (2015) doi: 10.1111/mmi.12843.
[2] Minamino, T. Protein export through the bacterial flagellar type III export pathway. <http://www.ncbi.nlm.nih.gov/pubmed/24064315>
Biochim Biophys Acta (2014)1843(8):1642-8. doi: 10.1016/j.bbamcr.2013.09.005.
[3] Makino et al. The Architecture of the Cytoplasmic Region of Type III Secretion Systems. <https://www.ncbi.nlm.nih.gov/pubmed/27686865> Scientific Reports 6, Article number: 33341 (2016) doi:10.1038/srep33341

Ariel J. Blocker, PhD, FRSB
Reader in Microbiology 
Wellcome Trust Investigator
Schools of Cellular & Molecular Medicine and Biochemistry
Biomedical Sciences Building
University of Bristol
University Walk
Bristol  BS8 1TD
United Kingdom

Email: ariel.blocker at bristol.ac.uk <mailto:ariel.blocker at bristol.ac.uk>
Tel office (D39a): +44 117 33 12063
Tel wetlab (D57/D59): +44 117 33 12404
Tel wetlab office (D53): +44 117 33 12059
Tel drylab (D51): +44 117 33 12097
Tel Tecnai20: +44 117 33 12357
Dept. fax: +44 117 3312091
Room: D39a
Personal webpage: http://www.bristol.ac.uk/cellmolmed/research/infect-immune/blocker.html <http://www.bristol.ac.uk/cellmolmed/research/infect-immune/blocker.html>
Group page: http://www.bristol.ac.uk/cellmolmed/research/infect-immune/blocker/ <http://www.bristol.ac.uk/cellmolmed/research/infect-immune/blocker/>
Postgraduate students searching for a PhD please look here:
http://www.bris.ac.uk/fmvs/gradschool/ <http://www.bris.ac.uk/fmvs/gradschool/>
Twitter: @T3Secreton

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