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. Author manuscript; available in PMC: 2015 Mar 1.
Published in final edited form as: J Biol Inorg Chem. 2013 Nov 30;19(3):319–334. doi: 10.1007/s00775-013-1068-3

Figure 3.

Figure 3

(A) Far-UV CD spectrum of HpUreF in 20 mM phosphate buffer in the absence (hollow circles) and in the presence of two equivalents of Ni2+ (hollow squares) per protein dimer. The best fit calculated for apo-HpUreF is represented as a solid line. Mean residue ellipticity units are degrees cm2 dm−1 residue−1; (B) Representative 1H-15N TROSY-HSQC spectrum of apo-HpUreF acquired at 900 MHz and 298 K; (C) Plot of the molar mass distribution of HpUreF in the absence (thick dots and line) and in the presence (thin dots and line) of two equivalents of Ni2+ per protein dimer. The solid lines indicate the Superdex-75 elution profiles monitored by the refractive index detector, while the dots are the weight-averaged molecular masses for each slice, measured every second.