Crystallization and preliminary X‐ray analysis of the LOV domain of the blue‐light receptor YtvA from Bacillus amyloliquefaciens FZB42

Light–oxygen–voltage (LOV) proteins play an important role in blue‐light‐dependent physiological processes in many organisms. The LOV domain of the blue‐light receptor YtvA from Bacillus amyloliquefaciens FZB42 has been purified and crystallized at 277 K using the sitting‐drop vapour‐diffusion method with 2‐ethoxyethanol as a precipitant. A data set was collected to 1.60 Å resolution from a single crystal at 100 K using synchrotron radiation. The LOV domain of YtvA crystallized in space group C 222 1 , with unit‐cell parameters a  = 64.95, b = 83.76, c = 55.81 Å. The crystal structure of the LOV domain of YtvA was determined by the molecular‐replacement method. The crystal contained one molecule per asymmetric unit, with a Matthews coefficient ( V M ) of 3.04 Å 3  Da −1 ; the solvent content was estimated to be 59.5%.