Services

We support users from project design to structure determination. Using the latest protein structure prediction software we provide an initial feasibility assessment and guide users toward the most promising designs.

Cloning
We use custom plasmid libraries combined with the SLIC (Sequence and Ligation Independent Cloning) system to quickly generate expression plasmids. This allows efficient screening of different hosts, tag types (His, Strep, etc.), and tag positions (N- or C-terminal).

Expression
We produce proteins in bacteria (E. coli), insect cells (Sf9 and Hi5), and mammalian cells (HEK293, Expi293), selecting the optimal system based on the target protein and experimental needs. E. coli is ideal for small proteins or constructs without post-translational modifications (PTMs). For protein complexes, we use MultiBAC and GoldenBAC systems in insect cells, allowing simultaneous expression proteins under individual promoters. Proteins requiring human specific PTMs are produced via transient transfection in HEK293/Expi293 suspension cells.

Purification
We use a wide range of affinity resins for gravity flow and FPLC columns. Our instruments include 3 AKTA Purifiers, 1 BioRad NGC system, and 1 AKTA Xpress system, all operated at 4°C. For analytical purposes, we have 2 AKTA micro systems with SEC columns and capillaries for micro-fractionation.

Other Services
We also perform routine protein production and purification services, including antibody purification using combined protein A/G and affinity strategies. We also produce the following departmental enzymes:

• Tn5 transposase (tagmentation, library prep)
• ProteinA-turboID (proximity labelling with Ab)
• pAG-Mnase (cut&run protocols)
• GFP-RNAseH
• Biotinylated anti-GFP nanobodies
• SENP^EU sumo protease
• GST-3C prescission protease
• His6-3C prescission protease
• TEV protease

We provide biophysical characterization of proteins and protein complexes.

We routinely assess protein quality using mass photometry and SEC-SLS to evaluate monodispersity and determine molecular weight.

We also offer guidance on protein stability, using thermal shift assays under different buffer conditions to identify the best storage or experimental conditions for further biophysical and structural studies.

Our biophysics services include measuring binding affinities for protein–protein and protein–ligand interactions (DNA, peptides, small molecules) using isothermal titration calorimetry (ITC),  fluorescence polarization (FP), and bio-layer interferometry (BLI).

Crystallizing proteins requires high-quality samples, careful planning, and a bit of luck. To maximize success, we offer an high-throughput crystallization platform.

Initial trials are set up using the Mosquito nanolitre-dispenser robot, allowing screening of 96 conditions with as little as 15 μl of sample. We typically test 3–5 commercially available crystallization screens at 20°C and 4°C, using a broad range of sparse and rational matrix conditions.

Optimization of initial hits can be performed with the robot in 96-well plates or manually in 24-well plates using hanging or sitting drop techniques, with tailored conditions based on the initial results.

For X-ray diffraction, we have routinely accesses to synchrotron sources, including the European Synchrotron Radiation Facility (ESRF, Grenoble, FR) and Swiss Light Source (SLS, Villigen, CH). We perform in house data processing using crystallographic softwares installed on our high-performance cluster.

We support users from project design to cryoEM structure determination.

We are equipped with a glow discharge unit and a Vitrobot Mark IV for in house grid preparation. We have routine access to a 200 kV microscope for grid screening and preliminary data collection. High-resolution data collection is performed at the CM01 beamline at the European Synchrotron Radiation Facility (ESRF, Grenoble, FR). 

We process data in-house using the latest cryoEM softwares, running on a dedicated multi-core and multi-GPU workstation.