Refolding Record:
Protein | |
---|---|
Protein Name | Lumazine synthase 2 |
Abbreviated Name | Lumazine synthase 2 |
SCOP Family | Lumazine synthase |
Structure Notes | |
Organism | Brucella abortus |
UniProt Accession | P61711 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Alpha/Beta |
Molecularity | Pentamer |
Construct | |
---|---|
Full Length | n |
Domain | aa.1-145 |
Chimera | n/a |
Variants | n/a |
Chain Length | 145 |
Molecular Weight | 15932.2 |
Pi | 6.39358 |
Molecular Weight | 15932.2 |
Disulphides | 0 |
Full Sequence |
MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD VPGAYEIPLH AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ VQLETEVPVL SVVLTPHHFH ESKEHHDFFH AHFKVKGVEA AHAAL
|
Notes | n/a |
Expression | |
---|---|
Report | Goldbaum FA, Polikarpov I, CauerhffAA, Velikovsky CA, Braden BC, Poljak RJ (1998) Mol Cell Endocrinol, 123, 175-178 |
Project Aim | Crystallography |
Fusion | None |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | BL21(DE3) |
Expression Temp | 37.0 |
Expression Time | 4 |
Expression Vector | pET11b |
Expression Protocol | Cultures were incubated in LB medium at 37degC, expression was induced with 1mM IPTG and cells were grown for 4h. |
Method of Induction | IPTG |
Cell Density at Induction | OD = |
Cell Disruption Method | Sonication |
Lytic Agent | None |
Pre-Refolding Purification | None |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Dilution |
Wash Buffer | n/a |
Solubilization Buffer | 50mM Tris, 5mM EDTA, 8M urea, pH 8.0 |
Refolding Buffer | 150mM NaCl, 10mM NaPhosphate pH 7.4, 1mM DTT |
Pre-Refolding Purification | None |
Tag Cleaved | no tag |
Refolding pH | 7.4 |
Refolding Temperature | 4.0 |
Protein Concentration | |
Refolding Time | 3 days |
Redox Agent | DTT |
Redox Agent Concentration | 1mM |
Refolding Protocol | The cells were sonicated and inclusion bodies werer dissolved in solubilization buffer at room temperature with overnight agitation. the protein was refolded by dialysis against refolding buffer during 3 days with several changes of buffer. The protein was then purified using a MonoQ column. |
Refolding Assay | Crystallography |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | |
Refolding Yield | |
Purity | |
Notes |