Crystallization and Preliminary X-Ray Diffraction Analysis of Recombinant Phosphoribosylpyrophosphate Synthetase I from Thermus thermophilus HB27

Crystals of phosphoribosylpyrophosphate synthetase from the thermophilic bacterium Thermus thermophilus (Tth PRPPS1 HB27), suitable for X-ray diffraction, were grown by the hanging-drop vapor-diffusion method. Before X-ray diffraction data collection, the crystals were transferred to a cryoprotectant solution and were flash-frozen in liquid nitrogen stream. These crystals were used to collect the X-ray diffraction data set on the European Synchrotron Radiation Facility (ESRF, France, ID23-1 beamline) at 100 K to 2.6 Å resolution, which was suitable for determining the three-dimensional structure of the enzyme.