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Summary of Services

  • Initial crystal screens
  • Additional crystal screens
  • Optimization trials to get improved crystals
  • Collecting X-ray data (using either local X-ray equipment or at a synchrotron beamline)
  • Processing X-ray data and solving structure
  • Selenomethionine crystal derivatives (sometimes needed to get phase information)
  • Protein expression and purification for X-ray crystallography, NMR and SAXS
  • Quickchange mutagenesis

Each project is unique, but below is a general outline of the process for crystallization and structure determination through the MIC:

1 — Contact the MIC to discuss the feasibility of your project. If project is suitable for crystallization trials, proceed as below.

2 — Client completes Sample Information Form and an Authorization for Services and Payment Form.

3 — Client provides MIC with ~10 mg of pure protein sample, at a concentration of ~10 mg/ml, in low ionic strength buffer near neutral pH, for initial screens.

4 — MIC personnel will screen sample for crystallization, unless client prefers to be trained to do this. If crystals are produced, MIC staff will collect information on unit cell and resolution of diffraction.

5 — If your protein is a candidate for structure determination, client may approach Dr. Lesa Beamer or Dr. Jack Tanner to discuss the possibility of a formal collaboration for structure solution by crystallography. These collaborations are at the discretion of the above faculty, and would be expected to lead to joint publications and grant funding.

If you have any questions, please contact Dr. Kamal Singh by email at or at 573-884-1281.

Additional Resources: