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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 A resolution using synchrotron radiation at SPring-8. The crystals are monoclinic and belong to space group P2(1), with unit-cell parameters a = 40.86, b = 95.76, c = 48.04 A, beta = 106.43 degrees. The calculated Matthews coefficient is approximately 2.1 A3 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.


Shotaro Tanaka, Yuuji Moriizumi, Makoto Kimura, Yoshimitsu Kakuta. Overproduction, purification and preliminary X-ray diffraction analysis of a sulfotransferase from Mycobacterium tuberculosis H37Rv. Acta crystallographica. Section F, Structural biology and crystallization communications. 2005 Jan 1;61(Pt 1):33-5

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PMID: 16508083

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