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

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....

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-04, Vol.59 (4), p.721-723
Hauptverfasser: Balbo, Paul, Oliveira, Marcos
Format: Artikel
Sprache:eng
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ACDS
acetate metabolism
acetyl-CoA decarbonylase synthase
CODH
methanogens
Ni/Fe-S protein
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container_title Acta crystallographica. Section D, Biological crystallography.
container_volume 59
creator Balbo, Paul
Oliveira, Marcos
description 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.
doi_str_mv 10.1107/S0907444903001987
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subjects ACDS
acetate metabolism
acetyl-CoA decarbonylase synthase
CODH
methanogens
Ni/Fe-S protein
title Crystallization and preliminary X-ray data of the α2ɛ2 subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex from Methanosarcina thermophila
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