Crystallization and preliminary crystallographic analysis of human common‐type acylphosphatase

Human acylphosphatase, an 11 kDa enzyme that catalyzes the hydrolysis of carboxyl phosphate bonds, has been studied extensively as a model system for amyloid‐fibril formation. However, the structure is still not known of any isoform of human acylphosphatase. Here, the crystallization and preliminary X‐­ray diffraction data analysis of human common‐type acylphosphatase are reported. Crystals of human common‐type acylphosphatase have been grown by the sitting‐drop vapour‐diffusion method at 289 K using polyethylene glycol 4000 as precipitant. Diffraction data were collected to 1.45 Å resolution at 100 K. The crystals belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a  = 42.58, b  = 47.23, c = 57.26 Å.