X-ray crystallography facility

X-ray crystallography is the method of choice for the determination of high-resolution macromolecular structures including protein, DNA, RNA and complexes therof. It is complemented by other techniques such as nuclear magnetic resonance (NMR) as well as cryo-electron microscopy (Cryo-EM). While NMR and Cryo-EM share limitations concerning the size of the molecules investigated, X-ray crystallography delivers structural information irrespective of size and on an atomic level.

With the Institute of Pharmaceutical Biotechnology and the X-ray crystallography facility we are closing a gap in structural biology research at Ulm University. We offer collaborational- or service-like operation modes.

The facility is equipped with a state-of-the-art nanodispenser (Mosquito Xtal3) and a liquid handling station for automated preparation of crystallization conditions and reformating screens (Hamilton MICROLAB Star) and microscopes for the inspection and documentation of crystals. The equipment is complemented by expert knowledge of crystal handling, data collection as well as structure solution.

For X-ray diffraction experiments we have regular access to beamlines of different european synchrotrons like ESRF (Grenoble, France), SLS (Villigen, Switzerland) or DESY (Hamburg, Germany).

The facility is established and run by the Institute of Pharmaceutical Biotechnology (Niessing lab Ulm) and headed by Dr. Thomas Monecke. Please contact us for collaborations, services or more details.

The usage regulations (Nutzungsordnung) of the X-ray crystallography facility can be downloaded here. The facility is listed in the DFG Research Infrastructure portal (DFG RIsources).


General sample requirements

  • purified protein from native or recombinant sources (E.coli, yeast, insect cells, mammalian cells)
  • typical concentration needed: 2-20mg/ml (protein dependent)
  • typical volume needed for a complete initial screening: 200nl/drop = 320µl total volume
  • required sample homogeneity >95% (SDS-PAGE)
  • monodisperse sample without aggregates (gel filtration, multi-angle light scattering)
  • pure sample without co-purified DNA/RNA contaminants (260/280nm ratio)
  • low salt concentration (as high as necessary, as low as possible)
  • low buffer concentration (typical 20 mM)
  • no phosphate buffers


Dr. Thomas Monecke
Crystallization Facility Coordinator
Office: 2.069 (N27)
Tel.: 0731 - 50 23163
Publication List


X-ray crystallography facility
James-Franck-Ring N27
Room 2.028 (N27)
Ulm University
89081 Ulm

Workflow of X-ray crystallographic structure determination

Equipment of the facility

Nanoliter crystallization robot
TTPlabtech Mosquito Xtal3


Leica binocular microscope for inspection and documentation of crystals

Leica M165 C with MC170 HD camera
Stereomicroscope for inspection and documentation of crystals


Hamilton MICROLAB Star
Fully programmable liquid handling station

Commercially available crystallization screens
Up to 1000 different crystallization conditions


Crystal storage dewar
Worthington HC35


Crystal incubator