Tag - cryo-EM

VACANCY: Research associate x 2 (MED01698)

Reference: MED01698
Date posted: 27 January 2020
Closing date: 05 March 2020

Two research associate positions are available to study new mechanisms in DNA replication and the epigenetic basis of chromatin structure.

Position 1:

The successful applicant should have expertise in protein biochemistry and structural biology and will employ in vitro reconstitution and cryo-electron microscopy to investigate either:

  1. Novel DNA replication mechanisms, or
  2. how epigenetics affect chromatin structure.

Position 2:

The successful applicant should have expertise in genomics and proteomics and will employ novel sequencing-based approaches together with proteomics to investigate either:

  1. Novel mechanisms in the initiation of DNA replication and DNA repair, or
  2. nucleosome/chromatin organisation and structure at a genome-wide level in order to understand gene regulation in health and disease.

Job details | Apply

New paper proposes lagging-strand DNA extrusion mechanism

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. Proceedings of the National Academy of Sciences of the United States of America 114, E9529-E9538.
Abstract | Full text |

New cryo-electron microscope produces first beam

The cryo-electron microscope installed on the Imperial College London Hammersmith Campus produces its first beam, coinciding, fittingly, with the award of the 2017 Nobel Prize in Chemistry, to Jacques Dubochet, Joachim Franck and Richard Henderson, “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution.”

London research consortium for cryo-EM awarded £3 million

The London consortium for cryo-EM (LonCEM), of which the The DNA Replication Group is a founding member, awarded £3 million to establish a new, state-of-the-art cryo-EM facility at the Francis Crick Institute. The award is part of a larger £20 million investment by the Wellcome Trust in cryo-electron microscopy to support world-leading structural biologists across the United Kingdom.

New paper establishes architecture of the OCCM complex

Sun, J.*, Evrin, C.*, Samel, S. A., Fernández-Cid, A., Riera, A., Kawakami, H., Stillman, B.†, Speck, C.†, Li, H.† (2013). Cryo-EM structure of a helicase loading intermediate containing ORC–Cdc6–Cdt1–MCM2-7 bound to DNA. Nature Structural & Molecular Biology 20, 944-951.
*Shared first authorship; †Corresponding authors
Abstract | Full text | Brookhaven National Laboratory Newsroom |