Refolding Record:
Protein | |
---|---|
Protein Name | Integrase |
Abbreviated Name | IN |
SCOP Family | Retroviral protease (retropepsin) |
Structure Notes | |
Organism | Mouse |
UniProt Accession | Q80SU2 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Beta |
Molecularity | Unknown |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 102 |
Molecular Weight | 11245.9 |
Pi | 10.7 |
Molecular Weight | 11245.9 |
Disulphides | Unknown |
Full Sequence |
KPLAAAYQDQQDQPVIPHPFRVGDTVWVRRHQTKNLEPRWKGPYTVLLTTPTALKVDGIAAWIHAAHVKAATTPPAGTASGPTWKVQRSQNPLKIRLTRGAP
|
Notes | n/a |
Expression | |
---|---|
Report | Jonsson CB, Donzella GA, Roth MJ. (1993) Biologycal Chemistry, 268, 1462-1469 |
Project Aim | Expression and charactrization |
Fusion | None |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | HMS174DE3 |
Expression Temp | 0.0 |
Expression Time | 3 h |
Expression Vector | pETllC or pETINHl |
Expression Protocol | Two liters of E. coli HMS174DE3 (Novagene) cells that harbored either pETllC or pETINHl were grown to 0.7-1.0 Am units, induced with 1 mM isopropyl-1-thio-@-D-galacto-pyranoside (IPTG), and grown an additional 3 h prior to harvesting cells. |
Method of Induction | IPTG |
Cell Density at Induction | OD 0.7-1.0 = 600 |
Cell Disruption Method | Not stated |
Lytic Agent | None |
Pre-Refolding Purification | Ni-NTA agrose chromatography |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Dialysis |
Wash Buffer | 10 column volumes of Buffer A/pH 7.8 |
Solubilization Buffer | 50 ml of Buffer A (10 mM Tris base, 0.1 M Na2HPO4, 0.1% Nonidet P-40, 10 mM B-mercaptoethanol, 100 mM NaC1, 10% glycerol, 4 M urea)/pH 7.8, |
Refolding Buffer | 3 to 0 M urea in 2 liters of 20 mM HEPES, pH 7.4, 1 mM dithiothreitol (DTT), 20% glycerol, 0.1% Nonidet P-40, 400 mM monopotassium glutamate |
Pre-Refolding Purification | Ni-NTA agrose chromatography |
Tag Cleaved | no tag |
Refolding pH | 7.4 |
Refolding Temperature | 25.0 |
Protein Concentration | n/a |
Refolding Time | 24 h |
Redox Agent | DTT |
Redox Agent Concentration | 1 mM |
Refolding Protocol | The cells were solubilized in 50 ml of Buffer A (10 mM Tris base, 0.1 M Na2HPO4, 0.1% Nonidet P-40, 10 mM B-mercaptoethanol, 100 mM NaC1, 10% glycerol, 4 M urea)/pH 7.8, with slow shaking for 1 h at room temperature. The slurry was centrifuged at 12,000 X g for 10 min, and the supernatant slowly applied to a 1-ml nickel nitrilotriacetate affinity column (Ni-NTA, Qiagen, Chatsworth, CA) pre-equilibrated with Buffer A/pH 7.8, at 4c. All manipulations from this point were performed at 4c. The column was washed with 10 column volumes of Buffer A/pH 7.8, followed by 10 column volumes of Buffer A/pH 6.3, to remove the majority of background E. coli proteins prior to elution of IN. These steps were followed by 10 column volumes of Buffer A/pH 5.9, and 10 column volumes of Buffer A/pH 4.5. IN protein eluted after 1 column volume of Buffer A/pH 4.5. Protein concentration was measured by the method of Bradford (24) (Bio-Rad). An alternative protocol, purification B, was developed which substituted the B-mercaptoethanol in Buffer A with dithiothreitol, designated Buffer B. A 10-ml Ni-NTA column was developed as above with stepwise pH elutions after the application of crude extracts of pETllC or pETINH1. The majority of the E. coli proteins eluted in the first wash with Buffer B/pH 7.8. IN protein eluted throughout the first 6 column volumes of the Buffer B/pH 6.3 elution step, and the first four fractions of the Buffer B/pH 5.9 elution step. No IN protein was eluted in the Buffer B/pH 4.5 step. In all purifications, column fractions were slowly renatured by a 24-h step dialysis from 3 to 0 M urea in 2 liters of 20 mM HEPES, pH 7.4,1 mM dithiothreitol (DTT), 20% glycerol, 0.1% Nonidet P-40, 400 mM monopotassium glutamate over 4 days. Fractions were frozen in liquid nitrogen and stored at -70 C. A specific activity of 2.2 units/mg was calculated for the pH 5.9 fraction purified in prification B. One unit is defined as 1 pmol of U5 substrate converted to autointegrants/min. |
Refolding Assay | SDS-PAGE,Phosophor Imager Analysis |
Refolding Chaperones | None |
Refolding Additives | Glycerol |
Additives Concentration | 20% |
Refolding Yield | n/a |
Purity | n/a |
Notes | n/a |