Protein Crystallization Service
The protein crystallization service can help researchers better understand the three-dimensional structure of proteins. Our company can provide you with the latest protein crystallization methods and technical analysis, which can make you better understand the structure and function of protein molecules, and also contribute to the development of new drugs for rare diseases.
Introduction to Protein Crystallization Technology
Protein crystallization is the method of forming a structured lattice of complex macromolecules of proteins, which makes proteins more stable and less volatile. The crystallized protein is usually studied by X-ray structural biology to better understand the three-dimensional structure of the protein. In addition, crystallization is an effective method of protein purification, which can protect the target protein from contamination by other proteins or external biological substances.
Fig.1 Schematic diagram of crystallization of protein monomers using a synthesis kit. (Abe, Satoshi, et al. 2022)
Protein Crystallization for Rare Diseases
- Pharmacodynamics of drugs for rare diseases
At present, in the field of rare disease drug research, protein crystallization technology has been successfully applied in the research and development of small molecule drugs, hormone drugs, and antibody drugs. Through the study of protein crystallization, the efficacy and toxicity of new drugs for rare diseases can be predicted, which provides strong support for drug development. - Development of rare disease drug production process
Protein crystallization can make certain proteins with hydrolases or protein phosphorylases more stable. It is helpful to study the molecular properties of enzyme drugs for rare diseases, to provide decision-making reference for process optimization in production.
Our Services
The development of protein-based drugs for the therapeutics of rare diseases requires an in-depth understanding of the variables and conditions that affect the crystallization process. Any change in the protein crystal suspension will directly affect the drug efficacy. Our company combines automated laboratory reactors with real-time in-situ analyzers to determine the effects of crystallization parameters on protein aggregation, growth, caking, fragmentation, and shape change, precisely controlling the crystallization process to optimize protein crystallization and scale-up production.
| Service | Feature |
|---|---|
| Molecular Replacement (MR) | MR is used when the protein under study has a homolog (sequence identity > 40%) whose structure is known. In this case, initial phases can be approximated from the known structure by its rotation and translation in the unit cell. |
| Multiple Isomorphous Replacement (MIR) | MIR is a way of determining phases by soaking the crystal in a heavy atom solution and then comparing the diffraction pattern of this derivative crystal to that of the native crystal. The heavy atoms scatter more strongly than other atoms in the structure and therefore contribute enormously to the diffraction, which makes it easy to locate them and calculate their scattering both in magnitude and in phase. |
| Single- or Multi-wavelength Anomalous Dispersion (SAD or MAD) | SAD or MAD involves the use of synchrotron radiation to excite the crystal at a single or multiple specific wavelengths. Most commonly, all methionine residues are replaced by selenomethionines in the protein. Selenomethionine contains selenium instead of a sulfur atom, which makes it a moderately effective anomalous scatterer. Phase information may be recovered by the analysis of phase shift. |
Project Workflow
Our company provides a one-stop protein crystallization service, the entire experimental process only requires you to provide the gene sequence. We are willing to work closely with our customers to develop the application of protein crystallization in the field of rare diseases. If you are interested in our services, please feel free to contact us for more details and quotation information of related services.
Reference
- Abe, Satoshi, et al. "Cell-free protein crystallization for nanocrystal structure determination." Scientific Reports 12.1 (2022): 16031.
All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.
