Crystallization and preliminary X-ray analysis of adenylylsulfate reductase 
from Archaeoglobus fulgidus

Roth, Annette; Fritz, Günther; Büchert, Thomas; Huber, Harald; Stetter, Karl Otto; Ermler, Ulrich; Kroneck, Peter M.H.

doi:10.1107/S0907444900013366

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Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus

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Roth, Annette
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Roth, A., Fritz, G., Büchert, T., Huber, H., Stetter, K. O., Ermler, U., et al. (2000). Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), D56(12), 1673-1675. doi:10.1107/S0907444900013366.

Cite as: https://hdl.handle.net/21.11116/0000-0007-0DB8-C

Abstract

A group of anaerobic microorganisms use sulfate as the terminal electron acceptor for energy conservation. The process of sulfate reduction involves several enzymatic steps. One of them is the conversion of adenylyl sulfate (adenosine-5′-phosphosulfate) to sulfite, catalyzed by adenylylsulfate reductase. This enzyme is composed of a FAD-containing α-subunit and a β-subunit harbouring two [4Fe–4S] clusters. Adenylylsulfate reductase was isolated from Archaeoglobus fulgidus under anaerobic conditions and crystallized using the hanging-drop vapour-diffusion method using PEG 4000 as precipitant. The crystals grew in space group P2₁2₁2₁, with unit-cell parameters a = 72.4, b = 113.2, c = 194.0 Å. The asymmetric unit probably contains two αβ units. The crystals diffract beyond 2 Å resolution and are suitable for X-ray structure analysis.