Abstract
ATP Sulfurylase (ATPS) catalyzes ATP (Adenosine-5'-triphosphate) and sulfate into adenosine 5'-phosphosulfate (APS) and pyrophosphate (PPi), which plays an important role in both assimmilatory and dissimlatory sulfate reduction. ATPS was purifued from Desulfovibrio gigas periplasmic part. SDS-page, UV wavescan, N-terminal sequencing, Synchrotron Radiation Circular Dichroism (SRCD) are used to identify and characterized ATP Sulfurylase. The crystallization condition was found and optimized to produce the crystal of ATP Sulfurylase. Xray diffraction of ATPS crystal allows structural determination that provides a better understanding of the zine containing enzyme. By the unit-cell parameter, the calculated Mattew’s coeffcient and solvent content are 2.33 (Å^3/Dalton) and 47.21%, respectively. Furthermore, Mattew’s coeffcient suggested that the presense of a monomer in the asymmetric unit. The initial linear R-factor is 0.064. The structure determination using MR and heavy atom method are in progress to elucidate its function.