Roth, A. and Fritz, G. and Buechert, T. and Huber, H. and Stetter, Karl Otto and Ermler, Ulrich and Kroneck, P. M. H. (2000) Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 56. pp. 1673-1675. ISSN 0907-4449
Full text not available from this repository. (Request a copy)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 alpha -subunit and a beta -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 P2(1)2(1)2(1), with unit-cell parameters a = 72.4, b = 113.2, c = 194.0 Angstrom. The asymmetric unit probably contains two alpha beta units. The crystals diffract beyond 2 Angstrom resolution and are suitable for X-ray structure analysis.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | POLYACRYLAMIDE GELS; PROTEINS; ARCHAEBACTERIA; BACTERIA; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 Mar 2022 16:58 |
| Last Modified: | 09 Mar 2022 16:58 |
| URI: | https://pred.uni-regensburg.de/id/eprint/41982 |
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