CEITEC Single Crystal X-ray Diffraction

Diffraction experiments with single crystal samples focused on determining the 3-D structure of (macro)molecules down to atomic resolution. Range of applicable molecular mass: from 102 up to 106, where the lower value covers molecules significant for nanotechnology, material science or pharmacology and upper limit covers biomacromolecules such nucleic acids, proteins and their complexes. Automated screening of crystallization conditions, optimisation of protein crystals growth.
The diffraction of X-rays in single crystal samples is the most important and – if an appropriate sample is available- also the fastest methodology currently available for the determination of atomic structures of molecules and/or macromolecules and their complexes. The Faculty of Science at Masaryk University has almost 20 years of experience with the diffraction laboratory focussed on small molecules. The new Core Facility is a coherent extension to new, macromolecular and biological studies of subjects with higher molecular masses. The bottleneck in diffraction techniques – time consuming preparation of protein crystals – will be overcome using a highly automated high throughput infrastructure for protein growth preparation, monitoring, and analysis. Centralised organisation of this instrumentation allows cost-effective use of resources and the exploitation of results even for untrained users.