Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Thermosynechococcus vestitus |
Crystallization (Comment) | Organism |
---|---|
using electron microscopy and small-angle x-ray scattering the structure of ChlH subunit is investigated. ChlH is a large, 148-kDa protein of 1326 residues, forming a cage-like assembly comprising the majority of the structure, attached to a globular N-terminal domain of 16 kDa by a narrow linker region. This N-terminal domain is adjacent to a 5 nm-diameter opening in the structure that allows access to a cavity | Thermosynechococcus vestitus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
148000 | - |
- |
Thermosynechococcus vestitus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermosynechococcus vestitus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Thermosynechococcus vestitus |
Synonyms | Comment | Organism |
---|---|---|
chelatase H subunit | - |
Thermosynechococcus vestitus |
ChlH | - |
Thermosynechococcus vestitus |