We determine the three-dimensional structure of soluble proteins up to a size of at least 20 kDa in fully automated fashion. An initial sample characterisation will be done to determine the feasibility. Result are delivered within 2 weeks.

• Structural coordinates (PDB file)
• Report of structure calculation statistics
• Sequence-specific assignment

• protein size < 20 kDa
• protein concentration: > 500 uM or > 100 uM in favorable cases
• isotope labelling: ¹⁵N, ¹³C, ¹H
• any typical biochemistry buffer (e.g. HEPES, TRIS, phosphate)
• salt concentration: up to 200 mM 

We determine the binding site of small molecule ligands on a protein at atomic resolution. Results are delivered within 2 weeks.

• Chemical shift perturbation data
• Structural visualisation of binding site
• Dissociation constant K _D , if in mM to uM range
• Sequence-specific assignment

• protein size < 20 kDa
• protein concentration: > 500 uM or > 100 uM in favorable cases
• isotope labelling: ¹⁵N,  ¹³C,  ¹H
• any typical biochemistry buffer (e.g. HEPES, TRIS, phosphate)
• salt concentration: up to 200 mM 
• Titratable ligand in separate sample with same buffer

We determine the interaction site of proteins at atomic resolution. Results are delivered within 2 weeks.

• Chemical shift perturbation data
• Structural model of protein-protein complex
• Dissociation constant K _D , if in mM to uM range
• Sequence-specific assignment

• protein size < 20 kDa
• protein concentration: > 500 uM or > 100 uM in favorable cases
• isotope labelling: ¹⁵N, ¹³C, ¹H
• any typical biochemistry buffer (e.g. HEPES, TRIS, phosphate)
• salt concentration: up to 200 mM 
• Second protein unlabelled in separate sample with same buffer

We characterise the backbone dynamics of proteins at the atomic level. Result are delivered within 2 weeks.

• Spin relaxation data
• Interpretation by model-free analysis
• Structural model of dynamics
• sequence specific assignment

• protein size < 20 kDa
• protein concentration: > 500 uM or > 100 uM in favorable cases
• isotope labelling: ¹⁵N, ¹³C, ¹H
• any typical biochemistry buffer (e.g. HEPES, TRIS, phosphate)
• salt concentration: up to 200 mM 

We characterise the conformational state of a biomolecule in different conditions and compare with reference states. Result are delivered within 1 week.

• 2D fingerprint spectra
• Quantification of conformational states

• protein size < 150 kDa
• protein concentration: > 100 uM 
• isotope labelling: selective ¹³C ¹H ₃ methyl labelling on ¹²C, ²H background
• any typical biochemistry buffer (e.g. HEPES, TRIS, phosphate)
• salt concentration: up to 200 mM 

Other services can be provided upon request. Please contact us for additional information.