“We need a people’s cryo-EM”

– Richard Henderson, Nobel Prize in Chemistry 2017

“When the world is in trouble, chemistry comes to the rescue!”

– Carolyn Bertozzi, Nobel Prize in Chemistry 2022

  • Experience the dynamic molecular architectures and conformations of samples first-hand.
  • Shape the future of molecular discovery with ease and ensure reproducibility.
  • Don’t stop at biochemical functional assays! Visualize the structures and contribute to scientific discovery and knowledge
  • Showcase your story by exploring and characterizing the structures.
  • Structures from homogeneous and heterogeneous samples.
  • Tagged or non-tagged protein complexes, protein-ligand complexes, biomolecules and viruses.
  • Case studies celebrating unbiased native biomolecular architectures and subcomplexes.

Precision structure determination now accessible, affordable, reproducible and scalable

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Type I restriction modification system (EcoR124I)

The first unbiased electron density map of the type I restriction modification system EcoR124I that enables bacteria fight the invading viral genome. The pentameric complex comprises two restriction endonuclease subunits, two methylation subunits and one specificity subunit.

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EcoR124I Methyltransferase

The first unbiased electron density map of the Mtase trimeric complex of EcoR124I. This complex forms when two methylation subunits (shown as deep pink) bind to the specificity subunit (shown as turquoise). The HsdM subunit homes the catalytic site for DNA methylation as well as the binding site for the methyl donor and restriction cofactor S-AdoMet to perform its main function of DNA modification by transferring a methyl group from the donor AdoMet.

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Active fully resolved HsdR of type I restriction-modification subunit

The HsdR subunit of the EcoR124I Type I restriction-modification system is crucial for the ATP-dependent translocation and subsequent cleavage of unmethylated foreign DNA, utilizing energy from ATP hydrolysis to translocate along the DNA and introduce double-strand breaks at distant sites. The HsdR subunit’s endonuclease activity is highly regulated through interactions with the HsdS and HsdM subunits, forming a functional holoenzyme that ensures only foreign DNA is targeted.

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