Science & Application
cryoWrite has been founded by scientists with long standing expertise in cryo-EM and sample grid preparation. They were and are driven by the conviction that a successful automated sample grid preparation is possible and will be a breakthrough in accelerating discovery in life science research.
cryoWrite continues to combine both, science & technology, and uses its expertise to listen to the needs and wishes perceived in the cryo EM community and provide innovative technological answers.
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Scientific Advances
Blot-free, nanoliter operation:
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Only ~2-5 nL of sample required per grid — three orders of magnitude less than traditional methods.
Controlled deposition:
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Enables tunable ice thickness via capillary-to-grid distance, writing speed, and humidity.
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Reproducibility comparable or superior to other commercial systems.
Multiple-writing modes:
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Double-writing boosts particle density 5–10× without higher concentration.
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On-grid mixing (two-line writing) enables time-resolved or ligand-binding experiments directly on the grid, demonstrated with streptavidin–desthiobiotin and NrS-1 + apoF co-deposition.
Reduced orientation bias:
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Grids of NrS-1 prepared with cryoWriter displayed more isotropic particle orientations (SCF 0.65 vs 0.45) than blotting-based methods, improving 3D reconstructions.
Integrated environmental control:
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Operates at dew-point temperature, avoiding condensation or sample drying, critical for consistent nanoliter handling.
3D reconstruction of TMV at 1.92 Å resolution. The filaments were deposited and vitrified with the cryoWriter. Data and movie courtesy: Claudio Schmidli, Thomas Braun group, Biozentrum, University of Basel. Electron Microscopy Databank entry: EMD-4628. Protein data bank: PDB-6R7M. More information on the preparation and data processing is found in the original publication in PNAS.
Scientific Versatility
High-resolution single particle reconstruction of various types of protein samples prepared using the cryoWriter.
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a) Tobacco mosaic virus (TMV)
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b) Horse spleen apoferritin (apoF)
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c) Transient receptor potential melastatin 4 (TRPM4) channel membrane protein.
For each sample from top to bottom:
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an atlas image, indicating the areas where data were collected by green boxes (scale bar = 200 μm);
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Representative cryo-EM micrograph (scale bars from left to right = 60 nm, 80 nm, 100 nm);
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2D class averages of picked particles (scale bars from left to right: 19 nm, 10 nm 16 nm);
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3D reconstructions with local resolution shown by the color scales (in Å); Representative regions in the 3Dreconstructions, with fitted atomic protein models.
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VH Chinmaya et al., EPFL/DCI, 2025
