Crystallization and preliminary X-ray data of the α2ɛ2 subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex from Methanosarcina thermophila

The α2ɛ2 subcomponent (218.6 kDa) of the 1.99 MDa acetyl‐CoA decarbonylase/synthase (ACDS) multienzyme complex is an Ni/Fe–S enzyme that catalyzes reversible CO2/CO reduction in the context of acetyl‐CoA synthesis. The ACDS complex is required for methanogenesis from acetate in methanogenic archaea. The α2ɛ2 subcomponent from Methanosarcina thermophila, grown on acetate, was purified and crystallized. The crystals were mounted in a capillary and diffracted to 4.0 Å resolution at room temperature. Different flash‐cooling approaches were attempted, all of which resulted in poor diffraction.