X-ray diffraction data of NAD-free SAHase from B. elkanii in complex with adenosine

Raw X-Ray synchrotron diffraction data for the crystal of NAD-free S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine. The diffraction images were collected to the resolution of 1.92 Å on the beamline BL14.1 at BESSY, Berlin, at 100 K using a Pilatus 6M detector. The data was recorded in one pass of 3000 images to resolution of 1.92 Å with crystal-to-detector distance 421.32 mm. The direct beam position was: x=1241 px, y=1260 px, oscillation angle was 0.1° and X-ray wavelength equal to 0.9184 Å.