CryoEM Services
The Power of Rosetta: Highest Atomic Accuracy Structures Actionable for Drug Discovery
Rosetta has pioneered major advances in the field of structure determination from CryoEM data. Major achievements in the CryoEM field using Rosetta include:
- Solving models otherwise impossible using other approaches
- Refining structures to far better effective resolution than other approaches
- Many high profile publications in journals such as Nature, Cell, and PNAS
The Power of Rosetta
Rosetta combines the world’s best protein structure refinement force field and approach with a demonstrably superior method for fitting a protein structure into a CryoEM derived map. The result is far better effective resolution than is possible with any other CryoEM refinement approach.
Cyrus employs multiple world experts in the field of applying Rosetta to CryoEM structure solution and refinement.
Cyrus scientists have co-authored several of the cutting edge Rosetta/CryoEM publications.
It is our priority to help your mission
We offer collaborative flexibility in model building, structure refinement, or complete turnkey services from prepared sample to fully refined structures.
- CryoEM data collection through partners
- Structure refinement into density
- Model building into density de novo
- Model building with modifications, such as carbohydrates
- Homology Modeling with CryoEM density
- Model completion for partly-built models
Rosetta CryoEM References
- Simon et al (1999) Proteins Supply 3 171-176
Ab initio protein structure prediction of CASP III targets using ROSETTA
- Rohl et al (2004) Methods in Enzymology 383 66-93
Protein structure prediction using Rosetta
- DiMaio et al. (2009) J Mol Biol 392 181-190
Refinement of protein structures into low-resolution density maps using Rosetta - DiMaio et al (2013) Protein Science 22 865-868
Cryo-EM model validation using independent map reconstructions - Song et al (2013) Structure 21 1735-1742
High-resolution comparative modeling with RosettaCM - Kim et al (2014) Proteins 82 208-218
One contact for every twelve residues allows robust and accurate topology-level protein structure modeling - DiMaio et al (2015) Nature Methods 12 361-365
Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement - DiMaio et al (2015) Nature Struct Mol Biol 22 642-644
The Molecular Basis for Flexibility in the Flexible Filamentous Plant Viruses - Hospenthal et al (2015) Cell 164 269-278
Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling
- Kudryashev et al (2015) Cell 160 952-962
Structure of the type VI secretion system contractile sheath
- Wang et al (2015) Nature Methods 12 335-338
De novo protein structure determination from near-atomic-resolution cryo-EM maps - Walls et al (2016) Nature Structure & Molecular Biology 23 899-905
Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy - Walls et al (2016) Nature 531 114-117
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer - Wang et al (2016) eLife 5 e17219
Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta - Frenz et al (2017) Nature Methods 14 797-800
RosettaES: a sampling strategy enabling automated interpretation of difficult cryo-EM maps
- James et al (2017) PNAS 114 4430-4435
CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel - Schoebel et al (2017) Nature 548 352-355
Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3