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Literature summary for 3.1.2.1 extracted from
- Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis (2013), Acta Crystallogr. Sect. F, 69, 1303-1306.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli as a His-tagged fusion protein | Neisseria meningitidis |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| acetyl-CoA hydrolase is crystallized using the hanging-drop vapour-diffusion technique at pH 8.5 and 17°C using ammonium phosphate as a precipitant. Optimized crystals diffract to 2.0 A resolution | Neisseria meningitidis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Neisseria meningitidis | A1KUS8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| using Ni-NTA chromatography | Neisseria meningitidis |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | crystal structure | Neisseria meningitidis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acetyl-CoA hydrolase | - |
Neisseria meningitidis |
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