Overproduction, purification and preliminary X-ray diffraction analysis of a sulfotransferase from Mycobacterium tuberculosis H37Rv.
Shotaro Tanaka, Yuuji Moriizumi, Makoto Kimura, Yoshimitsu Kakuta
Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Hakozaki 6-10-1, Fukuoka 812-8581, Japan.
Acta crystallographica. Section F, Structural biology and crystallization communications 2005 Jan 1Sulfotransferase 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.
Citation
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
Mesh Tags
Substances
PMID: 16508083
View Full Text
