MS07-02 - Crystallographic Enzymology: Using Synchrotroton Radiation for High Resolution in Space and Time


Thomas Schneider (European Molecular Biology Laboratory Hamburg, Germany) 

With the advent of highly brilliant synchrotron sources such as PETRA III, MAX IV (and a number ongoing or planned upgrades of other synchrotrons), it has become possible to produce X-ray beams optimally tailored to applications in structural enzymology. While highly homogenous and stable X-rays can be used to extract the best possible data from large (> 20 µm) crystals, micro-focus beams can be used to obtain data from small (< 20 µm) crystals. Being able to exploit small crystals is of particular value in the context of time-resolved crystallography as – in a pump-probe scenario - a homogeneous and synchronized triggering of a chemical reaction is often only possible for limited sample volumes. The routine availability of micro-focus X-ray beams on synchrotrons in combination with novel ‘serial’ sample presentation technologies (in many cases originating from experiments designed for XFELs) is now paving the way to a renaissance of pump-probe time-resolved macromolecular crystallography.

The EMBL beamline P14 on PETRA III (DESY, Hamburg) offers a wide range of beam properties and sample presentation modalities. We will discuss how high-resolution structural data can be obtained on large molecular machineries such as the 20S proteasome, how serial approaches can be used to extract structural data from micro-crystals, and how pump-probe time-resolved diffraction data can be collected on the new T-REXX endstation.