Cloned (Comment) | Organism |
---|---|
expressed in BL21(DE3) cells | Rattus norvegicus |
Crystallization (Comment) | Organism |
---|---|
crystallization in sitting drops at 25°C using a reservoir of 0.1-0.25 M ammonium acetate, 0.1 M tri-sodium citrate, pH 5.6, with 22-26% (w/v) polyethylene glycol 4000. The co-crystals with 5 mM are grown using a reservoir of 0.15 M ammonium sulfate, 0.2 M sodium cacodylate, pH 6.5, with 26% (w/v) polyethylene glycol 8000. The crystal sturcture, solved by SAD phasing using selenomethionine-substituted protein, yields a final refined model with r = 18.0 and Rfree = 20.8 at 1.5-A resolution. Data from a co-crystallization experiment with 5 mM cysteine shows structural changes in the binding pocket, they are determined to 1.5 A resolution (final r = 19.8 and Rfree = 22.4). | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | a selenomethionine-substituted cysteine dioxygenase is produced | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P21816 | native and selenomethionine-substituted cysteine dioxygnease | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | Cys93-Sgamma is covalently bound to Tyr157-Cepsilon2 forming a cysteinyl-tyronsine linkage. | Rattus norvegicus |
Purification (Comment) | Organism |
---|---|
all buffers are supplemented with 5 mM dithiothreitol to prevent oxidation of the selenomethionine | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
CDO | - |
Rattus norvegicus |