Overproduction, purification and preliminary X-ray diffraction analysis of a sulfotransferase from Mycobacterium tuberculosis H37Rv

Shotaro Tanaka, Yuuji Moriizumi, Makoto Kimura, Yoshimitsu Kakuta

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Sulfotransferase STF1 from the Mycobacterium tuberculosis H37Rv genome was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals diffract to 1.5 Å resolution using synchrotron radiation at SPring-8. The crystals are monoclinic and belong to space group P21, with unit-cell parameters a = 40.86, b = 95.76, c = 48.04 Å, β = 106.43°. The calculated Matthews coefficient is approximately 2.1 Å3 Da-1 assuming the presence of one molecule of STF1 in the asymmetric unit. A substrate-binding assay using a PAP-agarose column suggests that STF1 exhibits sulfotransferase activity.

Original languageEnglish
Pages (from-to)33-35
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number1
DOIs
Publication statusPublished - 2005

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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