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Piet Gros Lab

Bijvoet Centre for Biomolecular Research
Department of Chemistry, Faculty of Science
Utrecht University

email: p.grosuu.nl



Research Areas

Overview

Complement System

Plasma & Membrane Proteins

Crystallographic Method Development

Major Techniques

X-ray Crystallography

Cryo-Electron Microscopy

Biophysical Characterisation


Post-Doctoral Vacancy

We are currently seeking a postdoctoral researcher for cryo-EM studies of large protein complexes involved in cellular immunity.

My group has a long-standing track record at the frontiers of structural biology focussing on elucidating the molecular mechanisms that underlie biological processes with a major emphasis on human plasma-proteins and cell-surface receptors. The lab has an internationally strong reputation in uncovering the molecular mechanisms that underpin the complement system. We combine protein crystallography, cryo-electron microscopy, light microscopy, biochemical and biophysical assays to get a detailed picture of the molecular interactions that enable the complement system to discriminate between healthy self-cells and pathogens or dying/malignant cells.

We currently offer the opportunity for a postdoctoral researcher to join forces with us on an ERC funded project that investigates the correlation between levels of organisation within the membrane and complement efficacy. Most of the interactions we are looking into for this project are in the high nM to mM range and involve large flexible multi-domain proteins. So, the challenge for you as the candidate will be to find conditions/tricks that capture the complex of interest in a state that enables detailed structural analyses.

Principal tasks and responsibilities:

  • Deliver high quality protein samples for structural analyses;
  • Collect and analyse cryo-EM data;
  • Structure determination, atomic model building and validation;
  • Function as a go-to for PhDs and postdocs in the group for expert advice on all aspects of cryo-EM sample preparation, data collection and analyses;
  • Communicate you research findings within the group and to the larger scientific community.

We seek a highly motivated individual with the ability to run their project independently, but who also likes to also collaborate with and advice other members of our team.

Required knowledge/skills/abilities:

  • a PhD in structural biology or a closely related field;
  • Proven experience in cryo-EM;
  • Purification and analysis of protein complexes;
  • Excellent oral and written skills in English

Optional skills/abilities that are considered an advantage:

  • Protein crystallography;
  • Cryo-ET;
  • Molecular biology;
  • Experience with membrane proteins.

We offer a position for two years with the possibility of an extension to a maximum of 4 years. Full-time gross salary ranging from €2,839 to €4,474 in scale 10 of the Collective Labour Agreement Dutch Universities (CAO) plus 8% holiday bonus and 8.3% end-of-year bonus. More information about working at the Faculty of Science can be found here.


JBC cover

News flash

The article “Cryo-electron microscopy structure and potential enzymatic function of human six-transmembrane epithelial antigen of the prostate 1 (STEAP1)” by Oosterheert and Gros has been selected by the Journal of Biological Chemistry as the representative ‘Protein Structure and Folding’ article for the 2020 retrospective collection called "The year in JBC: 2020".

The STEAP1 structure was featured on the cover of this issue.


Research Highlights


Tetraspanin CD9/EWI-F
CD9::EWI-F

Cryo-EM structure of CD9 in complex with EWI-F; implications for Tetraspanin-enriched microdomain formation .

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More STEAPs
STEAP1

Structural and biochemical studies of STEAP1 suggest a role as modulator of iron(III) reduction.

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Oligomeric Properdin
FP-multi

Complement enhancement by oligomeric properdin explained by crystal structures of properdin and properdin/C3b-CTC complexes.

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Caught in the act
IgM-C1

Structures of IgM-C1-C4b complexes on liposomes revealed by cryo-EM tomography.

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Metal Homeostasis
STEAP4

Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.

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C1-IgG1 complex
C1q

C1 binds heterogeneously to IgG1-Fc hexamer complexes.

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Complement Regulation
C3b-Factor H-Factor I

Ternary complex C3b-FH-FI reveals molecular mechanisms underlying co-factor activity and complement-immune processing

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Complement Lysis
MAC vesicle

Heterogeneous MAC initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography.

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Complement Regulation
C3b regulator complexes

Regulators of complement activity mediate inhibitory mechanisms through common C3b-binding mode

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Complement Activation
IgG-C1 complex

Complement is activated by IgG hexamers assembled at the cell surface.

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Stem Cells
LGR5-Rspo1 dimer

Stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5

Stem Cells
ZRNF3-Rspo1 complex

Structures of Wnt-antagonist ZNRF3 and its complex with stem cell growth factor R-spondin 1; implications for signaling

Ensemble Refinement
ensemble model of 3K0N

Modelling dynamics in protein crystal structures by ensemble refinement.

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Videos & Lectures


For more videos see our Protein structure videos gallery

Links & Miscellaneous