Fig. 1: Comparison of the ANME-2 samples investigated in this study and the procedure of protein isolation by native purification and crystallisation. | Nature Communications

Fig. 1: Comparison of the ANME-2 samples investigated in this study and the procedure of protein isolation by native purification and crystallisation.

From: Atomic resolution structures of the methane-activating enzyme in anaerobic methanotrophy reveal extensive post-translational modifications

Fig. 1

Images of the bioreactor and flasks containing the respective freshwater and marine ANME-2 are presented. Close-ups of granular biomass of ANME-2d reducing nitrate and fluorescence in situ hybridisation labelled micrographs7 of the marine methanotrophic consortium (red for the archaeon and green for the sulfate-reducing partner, using specific probes) are shown. Purified MCR fractions are shown on the SDS-PAGE at the bottom of the figure next to the crystals obtained from each sample (top being MCR ANME-2dV and bottom ANME-2dO). For ANME-2c, the sample passed on SDS-PAGE corresponds to dissolved crystals, and a picture of the purification procedure can be examined in Supplementary Fig. S2. L stands for ladder. Purification procedures were performed once for ANME-2c and ANME-2dV and three times for ANME-2dO.

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