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 this 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 StarLetM) 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: 1-10mg/ml (protein dependent)
  • typical volume needed for a complete initial screening: 200nl per 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 low as possible as high as necessary)
  • low buffer concentration (typical 20 mM)
  • avoid phosphate buffers


You can see the Post-Doc of the Institute.

Dr. Thomas Monecke

Office: 2.069 (N27)

Tel.: 0731 - 50 23163

DECT: 0731 - 50 15163


X-ray crystallography facility

James-Franck-Ring N27

Room 2.028

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