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Core Facility – XTAL Protein Crystallization Platform

Protein structure determination by x-ray crystallography requires high quality single crystals. Obtaining such crystals is an empirical and labor-intensive process. Therefore, the protein crystallization platform has benn established in 2008 by the Cluster of Excellence CellNetworks and Prof. Dr. Irmgard Sinning (BZH). The DFG-registered core facility (RI570) sets up and monitors high-throughput crystallization trials at nano-liter scale with its state of the art crystallization robots and fully automated imaging systems.

Decorative Teaser Image: a shiny perfectly round bubble is glowing in rainbow colors. Inside of it, crystal structures shaped as rectangles or haxagons are placed right in the middle.

Project request

Our service is open to all researchers from Heidelberg University and the Health + Life Science Alliance Heidelberg Mannheim. External projects can be accepted upon discussion.

Timeline for Protein Crytallography Facility: First Contact, Research Plan, Platform Account, Sample Submission, Lab Work, Monitoring, Analysis and Results

Services & Equipment

SERVICES

We would like to achieve the best crystallization results with your protein. In our experience, a quick "protein check" prior to the first crystallization trials clearly enhances the success rate. Please contact us via xtals@bzh.uni-heidelberg.de.

Initial Screening

Identifying one or more initial crystallization conditions is the first step on the way to high-quality protein crystals. For this purpose the platform offers 20 "crystallization screens", i.e. compilations of 96 mixtures of various reagents like salts, polymers, and buffers.

Optimization

In order to obtain well diffracting high-quality crystals, it is often necessary to refine the initial crystallization conditions by adding additional chemicals to the inital mixture or by modification of the mixture recipe.

Monitoring

Crystallization plates are stored at 18°C or 4°C and automatically imaged according to a customisable schedule. The images can be inspected from your own computer via the Rock Maker Web interface or at our platform computers.

Equipment

The protein crystallization platform has highly specialized equipment for setting up crystallization experiments with a minimum amount of protein and for storing and monitoring the crystallization trials at several temperatures. Over 200 reagent stock solutions and in-house screens guarantee flexibility and reproducibility. 

Our facility is equipped with state-of-the-art robotics and imaging systems to ensure precise, high-throughput crystallization screening and monitoring. These include:

  • Formulatrix RockImager RI182 crystallization plate imaging system
  • ArtRobbins Phoenix RE nano-liter crystallization robot
  • Rigaku Minstrel HT imaging system and two Gallery 700 incubators
  • PerkinElmerJanus 4-channel liquid handling robot
  • Formulatrix MUVIS UV microscope
  • ArtRobbins Gryphon LCP crystallization robot

Further Information on our Equipment

Team

Tabelle

Portrait of a man with glasses

Dr. Jürgen Kopp
Facility Head

juergen.kopp@bzh.uni-heidelberg.de
+49 6221 54 4112

Portrait of a smiling woman

Britta Klem
Technical Assistant

britta.klem@bzh.uni-heidelberg.de  
+49 6221 54 4112

Portrait einer lächelnden Frau mit Brille

Prof. Dr. Irmgard Sinning
Scientific Director
AG Sinning

irmi.sinning@bzh.uni-heidelberg.de
 

Contact

Protein Crystallization Platform
Biochemiezentrum (BZH)
Room 265/266
Im Neuenheimer Feld 328
69120 Heidelberg

Email: xtals@bzh.uni-heidelberg.de
Phone: +49 6221 54 4112

Visit our Webpage

Selected publications

Tabelle

Kohler, S., Kopp, J., Maiti, S., Bujnicki, J. M. & Peschek, J. (2025). Structure of fungal tRNA ligase Trl1 with RNA reveals conserved substrate-binding principles. Nat Struct Mol Biol.
Fiorentino, F., Thoms, M., Wild, K., Denk, T., Cheng, J., Zeman, J., Sinning, I., Hurt, E. & Beckmann, R. (2025). Highly conserved ribosome biogenesis pathways between human and yeast revealed by the MDN1-NLE1 interaction and NLE1 containing pre-60S subunits. Nucleic Acids Res. 53.
Häge, F. R., Schwan, M., Conde González, M. R., Huber, J., Germer, S., Macrì, M., Kopp, J., Sinning, I. & Thomas, F. (2025). Strand-Swapped SH3 Domain Dimer with Superoxide Dismutase Activity. ACS Central Science. 11, 157-166.
Gerber, J. L., Morales Guzman, S. I., Worf, L., Hubbe, P., Kopp, J., and Peschek, J. (2024) Structural and mechanistic insights into activation of the human RNA ligase RTCB by Archease, Nature Communications 15, 2378.
Klein, M. A., Wild, K., Kisonaite, M., and Sinning, I. (2024) Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome. Nature Communications 15, 716.
Kubikova, J., Ubartaite, G., Metz, J., and Jeske, M. (2023) Structural basis for binding of Drosophila Smaug to the GPCR Smoothened and to the germline inducer Oskar. PNAS 120, e2304385120.

For further information on some of the protein structures recently elucidated using crystals grown at our protein crystallization platform, please check our structure gallery:

Protein Crystallization Platform Structure Gallery

Funding Resources

Funding for the Xtal Platform: BZH & Exzellenzcluster CellNetworks

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