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: Comparison of the ANME-2 samples investigated in this study and the procedure of protein isolation by native purification and crystallisation.The alt text for this image may have been generated using AI.

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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