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Figure 1
(a) SDS–PAGE analysis of protein purification of the B.c His6-TssA Nt1 construct. Lane M, Mark12 marker (labelled in kDa). Lane 1, cell debris. Lane 2, cell-free extract. Lane 3, flowthrough (Ni column). Lane 4, final preparation. (b) SDS–PAGE analysis of protein purification of the B.c SeMet MBP-TssA CTD construct. The protein, indicated by the arrow, is shown to be ∼90% pure in the final preparation samples and thus was used for crystallization. Lane M, Mark12 marker (labelled in kDa). Lane 1, cell-free extract. Lane 2, unbound material (amylose column). Lane 3, B.c SeMet MBP-TssA CTD. Lane 4, after MBP cleavage. Lane 5, after gel filtration. Lane 6, final preparation. (c) B.c His6-TssA Nt1 crystals grown in 0.16 M calcium acetate, 0.08 M sodium cacodylate buffer pH 6.5, 14.4%(w/v) PEG 8000, 20%(v/v) glycerol. (d) B.c TssA CTD crystals grown in 0.1 M sodium chloride, 0.1 M Tris pH 8.0, 15%(v/v) ethanol, 5%(v/v) MPD.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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