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Literature summary for 1.3.1.3 extracted from
- Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5beta-reductase from Digitalis lanata Ehrh (2006), Acta Crystallogr. Sect. F, 62, 186-188.
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | inspection of the MAD-phased electron-density map shows that 5beta-POR is a Rossmann-type reductase and the quality of the map is such that it is anticipated that a complete atomic model of 5beta-POR may readily be built | Digitalis lanata |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overproduced by the pQE expression system and transformed into Escherichia coli strain B834(DE3) | Digitalis lanata |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| by the hanging-drop method, at 2.7 A resolution, crystals belong to space group P43212, contain a single 5beta-POR molecule in the asymmetric unit and tend to diffract anisotropically, identification of six out of eight possible Se-atom positions | Digitalis lanata |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Digitalis lanata | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| to homogeneity by Ni–NTA affinity chromatography | Digitalis lanata |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5beta-POR | - |
Digitalis lanata |
| progesterone 5beta-reductase | - |
Digitalis lanata |
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