Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8.
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)).
Taguchi
Yuichi
Y
Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Hoseki
Jun
J
Kakuta
Yoshimitsu
Y
Fukuyama
Keiichi
K
D002942:Circular Dichroism; D003001:Cloning, Molecular; D003460:Crystallization; D004795:Enzyme Stability; D008970:Molecular Weight; D013430:Sulfate Adenylyltransferase / Q000737:chemistry* / Q000235:genetics; D016963:Thermus thermophilus / Q000201:enzymology*; D014961:X-Ray Diffraction
D013430:Sulfate Adenylyltransferase