Postdoctoral researcher associate

Postdoctoral researcher associate for CryoEM facility & Preparation Laboratory (CERIC Membership Fees project WP3)

Deadline: 06 September 2026

Careers / Research Area

Ref: DA/26/26 Background

Elettra Sincrotrone Trieste is an international multidisciplinary research center offering international users access to synchrotron and free-electron laser radiation for the characterization and processing of matter. The extremely high quality of the light sources and beamlines has set new performance records and has been producing results of great scientific and technological interest. In order to allow the laboratory to remain competitive in the next 20 years, an entirely new synchrotron radiation source - Elettra 2.0 - belonging to the new generation of storage rings (DLSR or Diffraction Limited Storage Ring) is being installed and will join the already operating free-electron source FERMI in the next months. The new source will exhibit a major increase in the brilliance and coherence fraction of the photon beams. The Elettra 2.0 optics is based on our enhanced symmetric six bend achromat structure (S6BA-E) with a 12-fold symmetry and an emittance of 200 pm-rad at 2.4 GeV. The new structure creates also straight sections in the arcs permitting the installation of additional insertion devices, thus increasing the number of beamlines. Existing beamlines are being upgraded and new beamlines constructed to take full advantage of the characteristics of Elettra 2.0. See for more information.

Beamline / Project / Activity description

In the framework of the aforementioned upgrade, new beamlines will be built, extending our life science programs . Elettra is the Italian Partner Facility of CERIC-ERIC ( which was recently upgraded though the “Pathogen Readiness Platform for CERIC-ERIC Upgrade” ( ) project, funded by the Italian government and coordinated by Area-Science Park. One of the main achievements of the project is the installation, at the Elettra premises in collaboration with IOM-CNR and IC CNR, a cryo-EM facility for single-particle analysis, cryo-electron tomography and micro-electron diffraction. This new facility will further expand structural biology activities at the site complementing the Structural Biology Laboratory (SB Lab) of Elettra Sincrotrone Trieste, and the new dedicated beamlines under construction with our partners (two Small Angle Scattering (SAXS) and one µdiffraction beamlines), thus providing an integrated environment for structural biology, combining synchrotron‑based techniques and advanced laboratory facilities and enabling integrative structural biology workflows.

The present position will contribute to developing and consolidating these capabilities, which will be made available to the international user community through the CERIC‑ERIC access program.

Job description

The successful candidate will work in a multidisciplinary team and will contribute to build effective synergies between the cryo‑EM facility, the µXRD/MX beamline, the SAXS beamline and the associated laboratories.

The successful candidate will work within the Structural Biology Laboratory with the objective to strengthen the sample‑preparation workflow for cryo‑EM single‑particle analysis (SPA) and supporting integrative structural biology studies for both in-house research and user‑support. The successful candidate will be primarily in charge of enforcing and operating the pipeline for expression, purification, biophysical characterization of protein samples and protein complexes and sample preparation for either MX or cryo‑EM SPA, with focus on protein targets. Main efforts will be devoted to the use of single‑particle cryo‑EM and MX techniques, with opportunities to exploit complementary methods such as SAXS, NMR and others.

The candidate is expected to actively contribute to the implementation of the following tasks and to exploit the acquired expertise for supporting MX and cryo-EM facility projects:

• developing and applying established and robust protocols to express and purify recombinant proteins and protein complexes (i.e. protein–protein, protein–nucleic acids), assessing protein quality for subsequent characterization and structural analysis;
• performing biochemical and biophysical assays to assess sample stability, folding and oligomerization state, as well as to investigate protein–ligand interaction properties;
• performing protein crystallization and crystal optimization using the robotic facility available in the Structural Biology Laboratory;
• providing samples and scientific input to support the installation and operation of a new “prep room” for cryo‑EM sample vitrification;
• performing cryo-EM grid preparation;
• becoming acquainted with data‑collection workflows for macromolecular crystallography and cryo‑EM, in close collaboration with