Crystallization of proteins, nucleic acids, and complexes
Description: For the subsequent experimental determination of the 3D structure at atomic level by diffraction analysis, (using the home source or synchrotron).
Input: At least 200 μl of sample, with a minimal macromolecule concentration of 5 mg/ml, optimally 10-20 mg/ml. Purity at least 95 %.
Output: Crystals suitable for diffraction analysis.
Time: Weeks to months (depending on the complexity of the project and the methods chosen).
Approximate price: on request
Determination of 3D structure of biological (macro)molecules at high resolution
Description: Single crystal X-ray diffraction. Measurement of diffraction data of molecular crystals, at cryo-conditions or at room temperature. Measurement in crystallization plates. Upon agreement, it is possible to measure diffraction of small molecule crystals.
Input: Single crystal of the molecule (in the crystallization plate or vitrified in liquid nitrogen) of size at least 50 μm.
Output: High resolution structure of the molecule or the complex, typically 1.5- 3.5 Å (atomic level). Diffraction data, symmetry space group, 3D maps of electron density, atomic coordinates of the molecule (PDB or mmCIF format).
Time: Weeks or months, depending on the project complexity
Approximate price: on request
