Single crystal X-ray diffraction data for Rhizobium radiobacter N-carbamoyl-beta-alanine amidohydrolase

Single crystal X-ray diffraction data for Rhizobium radiobacter N-carbamoyl-beta-alanine amidohydrolase collected from crystals produced as below:

Purified recombinant RrCβAA was concentrated to 15 mg/mL using a 10 kDa MWCO centrifugal concentrator (Vivaspin) and subjected to sitting drop vapor diffusion crystallization screening with commercial screens from Molecular Dimensions and Hampton Research. Drops of 100 nL protein plus 100 nL well solution were set up against wells containing 70 L of crystallisation solutions. After two weeks crystals were found in xxx condition. An optimisation screen based on this condition was set up in 24 well plates by varying the PEG1500 concentration and MMT buffer pH. Drops of 1 μL protein and 1 μL well solution were set up on plastic cover slips over wells containing 1 ml crystallisation solution. Crystals grew in a well solution containing 23 % (w/v) PEG1500 and 100 mM MMT pH 6.0. Crystals were harvested with a LithoLoop (Molecular Dimensions Limited) and transferred to a cryoprotection solution of well solution supplemented with 50 % PEG400. Cryoprotected crystals were flash cooled in liquid nitrogen.