The Frag Xtal Screen can help to develop new drug candidates against COVID-19 and other diseases.
The structural analysis of small fragments bound to a specific protein target allows a structure-based development of high-affinity lead candidates. Skip time-consuming prescreening and use crystallographic fragment screening as first screening approach!
Figure adapted from 
* binding efficiency = high binding energy / molecular mass
The Frag Xtal Screen was developed in cooperation with the HZB MX-group at BESSY II (AG Weiss) and the Institute of Pharmaceutical Chemistry, University of Marburg (AG Klebe).
It is ready to use and provides an easy entry into crystallographic fragment screening. With practical skills in transferring crystals and cryocooling, 96 distinct fragments can be screened within one week.
E-Mail Christin for technical inquiries or further information: email@example.com
 Huschmann et al. (2016) Structures of endothiapepsin-fragment complexes from crystallographic fragment screening using a novel, diverse and affordable 96-compound fragment library. Acta Cryst F 72:346.
 Schiebel et al. (2016) Six Biophysical Screening Methods Miss a Large Proportion of Crystallographic Discovered Fragment Hits: A Case Study. ACS Chem. Biol. 11:1693.
 Schiebel et al. (2015) One Question, Multiple Answers: Biochemical and Biophysical Screening Methods Retrieve Deviating Fragment Hit Lists. ChemMedChem 10:1511.
 Rees et al. (2004) Fragment-based lead discovery. Nature Reviews Drug Discovery 3:660.