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



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



Acta Crystallographica Section D Biological Crystallography 58(6 Part 2): 1054-1055



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 ANG resolution at 100 K using Cu Kalpha radiation. The crystal belongs to space group P1, with unit-cell parameters a = 107.5, b = 109.9, c = 119.4 ANG, alpha = 108.1, beta = 109.8, gamma = 91.9degree. The presence of eight molecules per asymmetric unit gives a crystal volume per protein mass (VM) of 2.4 ANG3 Da-1 and a solvent content of 48% by volume. A full set of X-ray diffraction data was collected to 2.9 ANG from the native crystal.

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Accession: 010401186

Download citation: RISBibTeXText

PMID: 12037315

DOI: 10.1107/s0907444902005875


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