Extended Data Fig. 4: Asymmetric unit content and B-factor profile of MtFsr.
From: Structures of the sulfite detoxifying F420-dependent enzyme from Methanococcales
a, The four homotetramers contained in the asymmetric unit of MtFsr are shown in cartoon and the 96 [4Fe-4S]-clusters, the 16 FADs (in yellow) and 16 sirohemes (in pink) are shown in balls and sticks. To our knowledge, MtFsr contains the highest number of clusters seen in an asymmetric unit so far. b, Superposition of all sixteen chains from the asymmetric unit in MtFsr, with an average rmsd of 0.14 Å for 514-Cα aligned. The N- and C-terminus of each chain are shown by a blue and red sphere, respectively. The models are coloured according to their B-factor values; blue to red indicate low to high B-factors, respectively. c, Averaged B-factor values (in black) for each residue from the 16 chains composing the asymmetric unit of MtFsr. The averaged root mean square deviations (rmsd, in red) of the corresponding Cα is overlaid on the same graph. Averaged rmsd were calculated by the software superpose57.
