Crystallization and preliminary X-ray data of the alpha2epsilon2 subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex from Methanosarcina thermophila.
The alpha(2) epsilon (2) 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 CO(2)/CO reduction in the context of acetyl-CoA synthesis. The ACDS complex is required for methanogenesis from acetate in methanogenic archaea. The alpha(2)epsilon(2) subcomponent from Methanosarcina thermophila, grown on acetate, was purified and crystallized. The crystals were mounted in a capillary and diffracted to 4.0 A resolution at room temperature. Different flash-cooling approaches were attempted, all of which resulted in poor diffraction.
Balbo
Paul
P
College of Pharmacy, Center for Structural Biology, University of Kentucky, USA.
Oliveira
Marcos
M
D000105:Acetyl Coenzyme A / Q000096:biosynthesis; D000445:Aldehyde Oxidoreductases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D017020:Methanosarcina / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000737:chemistry*; D021122:Protein Subunits / Q000737:chemistry; D014961:X-Ray Diffraction
D009097:Multienzyme Complexes; D021122:Protein Subunits; D000105:Acetyl Coenzyme A; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase