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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 P212121, with unit‐cell parameters a = 42.58, b = 47.23, c = 57.26 Å.
Acta Crystallographica Section F – Wiley
Published: Jan 1, 2006
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