Crystallization and preliminary crystallographic analysis of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix

Crystals of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix strain K1 have been grown at 291 K using ammonium phosphate as a precipitant. The diffraction pattern of the crystal extends to 2.4 Å resolution at 100 K using Cu Kα radiation. The crystal belongs to space group P1, with unit-cell parameters a = 107.5, b = 109.9, c = 119.4 Å, α = 108.1, β = 109.8, γ = 91.9°. The presence of eight molecules per asymmetric unit gives a crystal volume per protein mass (V_M) of 2.4 ų Da⁻¹ and a solvent content of 48% by volume. A full set of X-ray diffraction data was collected to 2.9 Å from the native crystal.