Projects

Proteins represent the functional interface of almost all biological reactions. The composition of those macromolecules made of some tens to thousands of amino acids is encoded within the DNA which could be expressed as a series of the four base pairs or its corresponding amino acid sequence. Since it is much more sophisticated to understand the function of proteins the three-dimensional structure is often essential to gain the necessary inside obtainable by protein crystallography, nuclear resonance spectroscopy (NMR) or small angle X-ray scattering (SAXS). While crystallography and NMR both enable higher resolutions up to single atoms the throughput however is restricted by an enormous preparative effort due to searching for reasonable crystallographic conditions or isotopic labeling. On the other hand SAXS just requires a sufficient amount of purified protein for the measurement of individual protein species, which in turn corresponds with the time and the material to be invested. The PURE-SAXS project aims to develop an automated microfluidic platform to purify proteins by gel electrophoresis towards SAXS analysis at the EMBL synchrotron facility in Hamburg. Due to the small dimensions of the microfluidic separation channels the overall processing time could be reduced by at least one order of magnitude while the required sample volume is scaled down from the microliter to the nanoliter range. In addition we aim to parallelize microfluidic elements within a single platform to yield an even greater sample throughput.