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3. Protein Crystallization and Structure Determination

NMR spectroscopy is a key analytical technique for structure elucidation of a wide range of materials from small molecules to compounds. The technique provides detailed molecular information that allows researchers have in-depth understanding of composition, chemical structure, morphology, and dynamics. NMR is particularly useful in analysis of pharmaceuticals, screening weak-binding compounds and developing into drug-like inhibitors for drug discovery. Supported by our NMR platform, Creative Biostructure offers high quality customized services ranging from production of labeled-proteins to acquisition and analysis of high-field NMR data for researchers in science and pharmaceutical industry.

NMR workflow

NMR services capabilities

• Compound structure determination
• Chemical composition analysis
• Molecular characterization
• Reaction kinetics examination
• Quality control
• Dynamics, disorder analysis
• Isotope-labeled protein production
• Quantitative analysis
• Drug screening and design
• NMR mapping for living cells
• Mapping structure of biological drugs by NMR

Why Creative Biostructure?
State-of-the-art instruments
Senior scientists with extensive exerience
Rapid turnaround time

Sample preparation guideline

• Labeling with isotopes: Protein NMR spectroscopy requires isotope enrichment, such as ¹⁵N, ¹³C, ³¹P, ¹⁹F in common. Samples with other isotope are also acceptable.
• Size: The molecular weight of biomacromolecule of a NMR sample is typically less than 50 KDa for high-resolution structure elucidation. Larger proteins or complexes can be studied to identify ligand/drug-binding site or to characterize the physical state.
• Amount: For solution NMR, a sample typically contains 1-10 mg/ml or 0.3 mM purified protein in a suitable buffer; for solid-state NMR, we require larger amount of samples, please talk to our specialist for more information.
• Stability: For most in-depth studies by NMR, the protein needs to be stable for several days at room temperature for data acquisition.

Please contact us to discuss your particular project.

Ordering Process

Reference
Xiao S., Capelluto D., (2015). Tom1 modulates binding of Tollip to phosphatidylinositol 3-Phosphate via a coupled folding and binding mechanism. Structure, 23: 1910-1920