Towards the crystal structure of glycerol dehydrogenase from Thermotoga maritima

The NAD+‐dependent glycerol dehydrogenase (EC 1.1.1.6) from the extremely thermophilic bacterium Thermotoga maritima has been crystallized in the presence of glycerol by the hanging‐drop vapour‐diffusion method using 2‐methyl‐2,4‐pentanediol (MPD) as the precipitating agent. Crystals of the enzyme c...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-05, Vol.58 (5), p.867-869
Hauptverfasser: Srinivasan, Vasundara, Ma, Kesen, Adams, Michael W. W., Newton, M. Gary, Rose, John P., Wang, Bi-Cheng
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The NAD+‐dependent glycerol dehydrogenase (EC 1.1.1.6) from the extremely thermophilic bacterium Thermotoga maritima has been crystallized in the presence of glycerol by the hanging‐drop vapour‐diffusion method using 2‐methyl‐2,4‐pentanediol (MPD) as the precipitating agent. Crystals of the enzyme complexed with NAD+ have also been obtained. The crystals belong to the tetragonal system with space group I422 and unit‐cell parameters a = 105.3, c = 134.5 Å. They diffract to a maximum resolution of 1.4 Å using synchrotron radiation (λ = 0.838 Å). Crystals of the enzyme–NAD+ complex diffract to 2.5 Å resolution using in‐house Cu Kα radiation.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444902005012