Crystallization experiments with 2-enoyl-CoA hydratase, using an automated `fast-screening' crystallization protocol
A convenient method for screening crystallization conditions using an automated fast‐screen protocol has been implemented and tested on an enoyl‐CoA hydratase. The crystallization solutions for the initial screening and subsequent optimizations are prepared using a crystallization robot. Enoyl‐CoA h...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1994-07, Vol.50 (4), p.443-447 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | A convenient method for screening crystallization conditions using an automated fast‐screen protocol has been implemented and tested on an enoyl‐CoA hydratase. The crystallization solutions for the initial screening and subsequent optimizations are prepared using a crystallization robot. Enoyl‐CoA hydratase (E.C. 4.2.1.17), purified from rat‐liver mitochondria, is one of the enzymes from the β‐oxidation pathway of fatty‐acid metabolism; it catalyzes the reversible hydration of 2‐trans‐enoyl‐CoA's to l‐3‐hydroxy‐acyl‐CoA's. Different crystal forms, diffracting to 3.0 Å, were obtained. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444994001277 |