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Welcome to the High Throughput

Crystallization Laboratory




This resource is open to all the members of the Partnership for Structural Biology (PSB) including EMBL, ESRF, ILL, IBS.

Access to this facility for external users is funded through the  inext logo   

In these pages you will find information and instructions about methods available on the platform.

If you want to use our services please register: User Registration page







For additional information please contact us at:

Phone: 0033 (0) 476 207425 

e-mail: htx@embl.fr


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Latest news

The symposium "Macromolecules in Action" will be held at the European Photon and Neutron (EPN) science campus in Grenoble, France, from 4-5 July 2019.
Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors published in Nat. Comm.
Automated pipelines for compound and fragment screening in Grenoble      The EMBL Grenoble, the ESRF and the iNEXT consortium are jointly offering access to automated pipelines for compound and fragment screening based on the CrystalDirect[1] technology and the MASSIF[2] beamlines. Access to these...

New CrystalDirect paper published in Acta Cryst D: Automated harvesting and processing of protein crystals through laser photoablation, Zander et al. Acta Cryst. (2016). D72, 454-466

Automated harvesting and processing of protein crystals through laser photoablation


Zander et al. Acta Cryst. (2016). D72, 454-466


New methods for crystal mounting, soaking and cryocooling contribute to bridging the automation gap between crystallization and X-ray data collection.



Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.


Link to the full article