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Figure 1
Purification of recombinant kallistatin by ion-exchange chromatography. The Sumo3-kallistatin fusion protein was cleaved with SENP2 and the mixture (lane S) was loaded onto a HiTrap SP column. The protein was eluted with an NaCl gradient from 0 to 1 M, measuring the absorbance at a wavelength of 280 nm (a). Flowthrough (FT) and fractions from elution were analysed by SDS–PAGE (b). Fractions from peak I (13 and 14) and peak II (15–17) were pooled separately and subjected to crystallization trials. Lane M contains molecular-weight marker (labelled in kDa).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 71| Part 9| August 2015| Pages 1135-1138
doi:10.1107/S2053230X15012893
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