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Updated: Sep 20, 2026
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus
Yuichi Taguchi1, Jun Hoseki, Yoshimitsu Kakuta
1Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Abstract:
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 A, beta = 95.4 degrees. Diffraction to better than 2.5 A resolution was obtained using synchrotron radiation at SPring-8. The asymmetric unit most probably contains two subunits (V(M) = 3.48 A(3) Da(-1)).
