ATP sulfurylase catalyzes the reaction of inorganic sulfate with ATP, producing adenosine-5′-phosphosulfate (APS) and pyrophosphate. A probable ATP sulfurylase (MW = 38.8 kDa) from Thermus thermophilus HB8 was overproduced in Escherichia coli and purified. It was crystallized in the presence of 5 mM APS by the batch method. The crystal was monoclinic, space group P2 1, with unit-cell parameters a = 68.8, b = 61.2, c = 128.6 Å, β = 95.4°. Diffraction to better than 2.5 Å resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (VM = 3.48 Å3 Da -1).
|ジャーナル||Acta Crystallographica - Section D Biological Crystallography|
|出版ステータス||出版済み - 9 1 2003|
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