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Protein Crystallization

Creative Biostructure offers high-throughput UniCrys™ crystallization services with our state-of-the-art facilities and has developed an X-ray crystallography pipeline including all the stages from gene synthesis to structure determination. Our experienced scientists can teamwork with customers and accelerate the research progress.

Figure 1. Photos of  protein crystals Figure 1. Photos of protein crystals

X-ray crystallography is a scientific technique of determining the positions and arrangements of atoms in a crystal. Beams of X-ray diffract into various specific directions when they strike a crystal, forming a diffraction pattern that can be interpreted into the three-dimensional structure of macromolecules. Since the first determined protein structure – myoglobin – in 1958, X-ray crystallography has become the most significant and useful tool for protein structure determination. Nowadays, more than 115,000 protein structures have been deposited into the Protein Data Bank and about 90% of them are by X-ray, suggesting its overwhelming advantages in protein structure study.

The key step in X-ray crystallography is the crystallization process. Since each protein has its unique physical and chemical properties, the initial crystallization screening can be very costly and time consuming. However, by taking advantages of our in-house X-ray diffraction platform, Creative Biostructure can provide the most efficient and economical strategies. The detailed services we provide are summarized in Table 1.

Table 1. Protein crystallization services at Creative Biostructure

Service Feature
Co-crystallization Co-crystallization retains the unique crystalline structures with their multiple components (e.g., proteins, DNA/RNA, chemical compounds, metal ions).
Peptide Crystallization Great for crystallization of small peptides, especially flexible peptides without predefined conformation.
Viral Envelope Glycoprotein Crystallization Maintaining the prefusion state of viral envelope glycoprotein and cellular membrane, with activation of fusogenic conformational changes.
Electron Crystallography Electron crystallography is a powerful technique for the study of membrane protein structures and functions in a lipid environment.
Crystallization Chaperone Strategies Co-crystallization of challenging membrane proteins targets with covalent or non-covalent soluble protein chaperones.
Trace Fluorescent Labeling Crystallization Great for the detection and identification of crystals by covalently labeling a fluorescent probe on the protein. The fluorescent probe is concentrated along with the formation of crystals, and producing fluorescent that is visually detectable under microscopic field.
Lipidic Cubic Phase (LCP) Crystallization LCP has a membrane-mimetic matrix suitable for stabilization and crystallization of membrane proteins in lipidic environment.
Controlled in Meso Phase (CLMP) Crystallization CIMP stabilizes membrane proteins in the meso phase and allows for direct monitoring of phase transformation and crystallization events.

The structural biology team at Creative Biostructure carries out high-resolution structure determination by using both in-house X-ray facility (for trial and optimization) and synchrotron light source (for data collection). High-resolution X-ray data, high-quality density maps, protein structures and statistics will also be made available for the purpose of publication and subsequent studies.

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  1. Rohani S, et al. “Control of the product quality in batch crystallization of pharmaceuticals and fine chemicals. Part 1: design of the crystallization process and the effect of solvent”. Org Res Proc Dev, 2005, 9(6): 858–872.
  2. Rohani S, et al. “Control of the product quality in batch crystallization of pharmaceuticals and fine chemicals. Part 2: external control”. Org Res Proc Dev, 2005, 9(6): 873–883.

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