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

The crystallization of the LOV domain of the blue-light receptor YtvA from B. amyloliquefaciens FZB42 is described. The crystals diffracted to 1.60 Å resolution. 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 C222₁, 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 ų Da⁻¹; the solvent content was estimated to be 59.5%