Structural Characterization

Protein Crystallography

Our protein crystallography services start with high-purity proteins (often produced by our own protein production team). With our fully automated platform, we can rapidly and reliably generate and optimize diffraction crystals for x-ray, including those with known and unknown crystallization conditions (novel, reproduction, membrane and fragment proteins).

About Protein Crystallography

Protein Crystallography Services

Helix’s protein crystallography services offer unmatched flexibility and scalability, providing scientists with timely and cost-effective options for proteins that require varying dispensing volumes and incubation temperatures. Helix also provides access to an extensive array of more than 50 commercial crystallization screens to explore diverse chemical spaces when crystals aren’t forming.

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Commercial Crystallization Screening

Pure, concentrated protein is automatically placed into humidity-controlled 96-well plates containing a variety of commercial crystallization conditions, which encourages protein crystal formation. Multiple robot configurations allow for lower-volume dispensing, as little as 50 nanoliters, and the option of using different incubation temperatures further increases screening flexibility.

Plate  Monitoring

Following commercial monitoring set up, plates are routinely screened with either an automated imager (ARI CrysCam CCUV) or light microscope (Leica M205C) to identify crystal hits. UV imaging in the CrysCam is then used to confirm whether the crystals are protein or salt.

Crystal Optimization

To ensure viable crystals are of suitable quality for x-ray diffraction, Helix uses a multitude of screening techniques including gradient, temperature, and cryo among others. Expertise in using DragonFly liquid dispensing robotics for optimization screens increases efficiency and condition accuracy while offering the highest reproducibility and quality.

X-Ray Data Collection

Once crystals are optimized, samples move to the synchrotron for x-ray screening via diffraction rastering technology, and, if data is of sufficient quality, a high-resolution data set will be collected on the crystal. Access to multiple beamtime slots (in several locations for maximum flexibility) puts the world's highest-quality beamlines within reach. After data collection, processing is done using Helix's state-of-the-art structure solution automation pipeline.

Structure Solution and Refinement

During this final stage, Helix experts assist with creating an electron density map to fully resolve the protein model. Going beyond simple transmission of data, Helix uses advanced software (Phenix, CCP4) and gene-to-structure expertise to deliver publication-ready structures of the highest quality.

Never feel lost in the process again

Throughout the protein crystallization process, project status is communicated weekly. The Helix   team provides detailed technical project reports at the end of each stage.

"We have consistently been impressed by Helix's expertise, quality, speed, and thoughtfulness throughout our work together. They have proven to be an ideal partner in our structural biology projects, consistently delivering impressive results and maintaining excellent communication every step of the way."

"Helix Biostructures has been delivering exceptional protein production and characterization services to us in the agricultural biotechnology sector. Our work together is defined by a shared dedication to excellence and an in-depth knowledge of the international regulations and standards necessary for the deregulation of biotechnological crops. Our collaboration makes a substantial contribution to our clients' endeavors in sustainably offering biotechnological solutions for crop protection and increased production."

"Collaborating with Helix to elucidate the structure of our therapeutic antibody in complex with its antigen through Cryo-EM was very valuable for our research. Their expertise in protein sciences and structural biology gave us detailed insights into the antibody-antigen allosteric mechanism, advancing our understanding significantly. The data they provided exceeded our expectations and contributed to the publication of a high-impact paper. The professionalism and technical skill of their team made the entire process smooth and efficient."

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