Flawless Crystals of a Biofuels Catalyst

Determination of the three dimensional structure of a protein at atomic scale resolution is the ‘holy grail’ for biochemists who wish to understand how a protein functions. To determine the structure, one must first crystallize the protein, then bombard the crystal with high energy x-ray beams and interpret the diffraction pattern. By far the most energy intensive part of the process is identifying the proper conditions in which the protein forms uniform and regular crystals. Here we have crystallized a protein which has novel application as a biocatalyst for alternative fuel production from plant residues. The protein was derived from a bacterium in the cow’s first stomach, the rumen, which represents one of the most efficient systems in nature for bioconversion of plant material. The data derived from this crystal will provide us with unique insight into how a bacterium in this complex microbial ecosystem extracts energy from plant biomass and will allow us to harness this potential for future biofuels production.