Refolding Record:
Protein | |
---|---|
Protein Name | Quinolinate synthetase |
Abbreviated Name | QS |
SCOP Family | Unknown |
Structure Notes | |
Organism | Escherichia coli |
UniProt Accession | P11458 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Unknown |
Molecularity | Monomer |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 352 |
Molecular Weight | 38240.8 |
Pi | 5.19323 |
Molecular Weight | 38240.8 |
Disulphides | Unknown |
Full Sequence |
MSVMFDPDTAIYPFPPKPTPLSIDEKAYYREKIKRLLKERNAVMVAHYYTDPEIQQLAEE
TGGCISDSLEMARFGAKHPASTLLVAGVRFMGETAKILSPEKTILMPTLQAECSLDLGCP
VEEFNAFCDAHPDRTVVVYANTSAAVKARADWVVTSSIAVELIDHLDSLGEKIIWAPDKH
LGRYVQKQTGGDILCWQGACIVHDEFKTQALTRLQEEYPDAAILVHPESPQAIVDMADAV
GSTSQLIAAAKTLPHQRLIVATDRGIFYKMQQAVPDKELLEAPTAGEGATCRSCAHCPWM
AMNGLQAIAEALEQEGSNHEVHVDERLRERALVPLNRMLDFAATLRG
|
Notes | n/a |
Expression | |
---|---|
Report | Ceciliani F, Caramori T, Ronchi S, Tedeschi G, Mortarino M, Galizzi A. (2000) Protein Expression and Purification, 18, 64-70 |
Project Aim | Functional Studies |
Fusion | None |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | TOP10 |
Expression Temp | 37.0 |
Expression Time | 5h |
Expression Vector | pTrcHisA |
Expression Protocol | unknown |
Method of Induction | Not Stated |
Cell Density at Induction | OD = |
Cell Disruption Method | Sonication |
Lytic Agent | None |
Pre-Refolding Purification | None |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Dialysis |
Wash Buffer | 50mM Tris-HCl pH 8.0 |
Solubilization Buffer | 50mM Tris-HCl, 10mM EDTA, 0.1mM PMSF, 4M urea, pH 8.0 |
Refolding Buffer | 50mM Tris-HCl, 10mM EDTA, 10% glycerol |
Pre-Refolding Purification | None |
Tag Cleaved | no tag |
Refolding pH | 8.0 |
Refolding Temperature | 4.0 |
Protein Concentration | 1mg/ml |
Refolding Time | 24h |
Redox Agent | None |
Redox Agent Concentration | n/a |
Refolding Protocol | The solubilized material was dislysed against 50mM Tris-HCl, 10mM EDTA, 10% glycerol and 2M urea pH 8.0 for 5h. Subsequently the refolding buffer was changed to 50mM Tris-HCl, 10mM EDTA, 10% glycerol pH 8.0. After 24h the solution was centrifuged and the supernatant was further purified by anio exchange chromotography. |
Refolding Assay | Enzyme activity |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | NULL |
Refolding Yield | 25mg/L culture |
Purity | many strong bands on SDS PAGE |
Notes |