Overproduction, crystallization and preliminary X-ray diffraction analysis of probable ATP sulfurylase from Thermus thermophilus HB8

Yuichi Taguchi, Jun Hoseki, Yoshimitsu Kakuta, Keiichi Fukuyama

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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 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).

Original languageEnglish
Pages (from-to)1645-1647
Number of pages3
JournalActa Crystallographica - Section D Biological Crystallography
Volume59
Issue number9
DOIs
Publication statusPublished - Sep 1 2003

All Science Journal Classification (ASJC) codes

  • Structural Biology

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