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. 2005 Jan 1;61(Pt 1):33-5.
doi: 10.1107/S1744309104022328. Epub 2004 Sep 25.

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

Shotaro Tanaka  1 , Yuuji Moriizumi, Makoto Kimura, Yoshimitsu Kakuta
Affiliations

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

Shotaro Tanaka et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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 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.

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Figures

Figure 1
Figure 1
SDS–PAGE of PAP–agarose assay. The arrow indicates the eluted STF1.
Figure 2
Figure 2
Crystals of STF1. Scale bar: 0.1 mm.
Figure 3
Figure 3
Diffraction pattern of the STF1 crystals. The frame edge is at 1.5 Å resolution.
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