Raw X-ray diffraction data of SAHase from Bradyrhizobium elkanii in complex with adenosine

Raw X-Ray synchrotron diffraction data for the crystal of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine. The diffraction images were collected to the resolution of 1.95 Å on the beamline BL 14.2 at BESSY, Berlin, at 100 K using a MAR225 detector. The data was recorded in one pass of 300 images to resolution of 1.95 Å with crystal-to-detector distance 200 mm. The direct beam position was: x=1531 px, y=1535 px, oscillation angle was 0.3° and X-ray wavelength equal to 0.918 Å.