3.1.6.1	crystals of arylsulfatase are obtained at a pH of 6.3 by hanging drop vapour diffusion method. The three-dimensional structure is determined to 1.3 A resolution in the space group C2. The asymmetric unit contains two monomers	663417	
3.1.6.1	full quantum chemical study performed at the density functional level, based on PDB entry 1HDH. The enzyme is able to catalyze the hydrolysis of the original 4-nitrophenyl sulfate substrate and the promiscuous 4-nitrophenyl phosphate.Only some steps of the promiscuous reaction are identical to those in the native process. Differences concern mainly the last step in which the His115 residue acts as a general base to accept the proton by the O atom of the FGly51 in the 4-nitrophenyl sulfate, whereas in 4-nitrophenyl phosphate, the Asp317 protonated residue works as a general acid to deliver a proton by a water molecule to the oxygen atom of the C-O bond	729602