a postdoctoral position is available at Imperial College London.
The Speck Lab works on the mechanism of eukaryotic chromosome replication. We are looking for a passionate researcher interested in investigating molecular machines.
The ideal candidate will have Structural Biology or Biochemistry expertise. Cryo-EM experience would be an advantage, but is not an absolute requirement.
Research framework and support structure:
1.) Excellent access to cryo-EM instruments: 1 Krios microscope equipped with K3 detector; multiple 200kV and 100kV microscopes for cryo-EM grid screening; supported by outstanding facility manager and senior investigator scientist.
2.) The group consists of >10 members, 7 postdocs, 2 students, including senior biochemical research scientist and lab manager that support protein _expression_ and purification.
3.) The lab is fully equipped for biochemistry (2 AKTAs, multiple temperature controlled shakers), cryo-EM data processing (GPU cluster and storage array) and generously supported by the Wellcome Trust and multiple BBSRC grants.
4.) Access to state-of-the-art facilities including Mass Spectrometry, Structural Biology and Bioinformatics.
5.) The candidate will receive direct mentoring by the group head on grant applications, writing of manuscripts and project design.
Interested individuals are welcome to contact me directly for more information.
here are a few links:
The BBSRC funded 3-year position:
Closing date: 07 October 2018
Noguchi Y*, Yuan Z*, Bai L*, Schneider S, Zhao G, Stillman B#, Speck C#, Li H# (2017) Cryo-EM structure of Mcm2-7 double hexamer on DNA suggests a lagging strand DNA extrusion model PNAS, Nov 7;114(45):E9529-E953
Riera A, Barbon M, Noguchi Y, Reuter LM, Schneider S, Speck C (2017) From structure to mechanism – understanding initiation of DNA replication Genes & Development, Jun 1;31(11):1073-108
Yuan Z*, Riera A*, Bai L*, Sun J*, Nandi S, Spanos C, Chen ZA, Barbon M, Rappsilber J#, Stillman B#, Speck C# and Li H# (2017) Structural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1 Nature Structure & Molecular Biology, Mar;24(3):316-32
Chang F, Riera A, Evrin C, Sun J, Li H, Speck C*, Weinreich M* (2015) Cdc6 ATPase activity disengages Cdc6 from the pre-replicative complex to promote DNA replication eLife, Aug 25;4
Samel AS, Fernández-Cid A, Sun J, Riera A, Tognetti S, Herrera MC, Li H, Speck C (2014) A unique DNA entry gate for regulated loading of the eukaryotic replicative helicase onto DNA Genes & Development, Aug 1;28(15):1653-6
Sun J*, Fernandez-Cid A*, Riera A*, Tognetti S, Yuan Z, Stillman B#, Speck C#, Li H# (2014) Structural and mechanistic insights into Mcm2-7 double-hexamer assembly and function Genes & Development, Oct 15;28(20):2291-30
Sun J*, Evrin C*, Samel S, Fernández-Cid A, Riera A, Kawakami H, Stillman B#, Speck C#, Li H# Cryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA (2013) Nature Structure & Molecular Biology, August 5, (20), 944–951
Fernández-Cid A, Riera A, Tognetti S, Herrera MC, Samel S , Evrin C, Winkler C, Gardenal E, Uhle S, Speck C. (2013) An ORC/Cdc6/MCM2-7 complex is formed in a multistep reaction to serve as a platform for MCM2-7 double-hexamer formation Molecular Cell, Volume 50, Issue 4, 577-588, 18 April
Professor Christian Speck, PhD, FRSB
Chair in Genome Biochemistry & Molecular Biology
Wellcome Trust Investigator
Imperial College London
Faculty of Medicine
Institute of Clinical Sciences (CRB room 3006)
Hammersmith Hospital Campus
Du Cane Road
London W12 0NN
Tel: 0044 20 8383 3387
Mobile: 0044 796 181 5557
Skype ID: dna_rep
Imperial College website: www.imperial.ac.uk/people/chris.speck
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