Refolding Record:
Protein | |
---|---|
Protein Name | Light harvesting complex II |
Abbreviated Name | LHC II |
SCOP Family | Unknown |
Structure Notes | |
Organism | Arabidopsis thaliana |
UniProt Accession | P04777 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Unknown |
Molecularity | Trimer |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 236 |
Molecular Weight | 24863.2 |
Pi | 5.11814 |
Molecular Weight | 24863.2 |
Disulphides | 0 |
Full Sequence |
RKTVAKPKGPSGSPWYGSDRVKYLG
PFSGESPSYLTGEFPGDYGWDTAGLSADPETFARNRELEVIHSRWAMLGALGCVFPELLA
RNGVKFGEAVWFKAGSQIFSDGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRVAGN
GPLGEAEDLLYPGGSFDPLGLATDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGP
IENLADHLADPVNNNAWAFATNFVPGK
|
Notes | n/a |
Expression | |
---|---|
Report | Standfuss and Kühlbrandt (2004) J Biol Chem, 279, 36884-36891 |
Project Aim | Structure-Function |
Fusion | C-terminal hexahistidine tag |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | BL21, XL1-blue |
Expression Temp | 37.0 |
Expression Time | 4h |
Expression Vector | pET 20b, pDS12 |
Expression Protocol | unknown |
Method of Induction | Not Stated |
Cell Density at Induction | OD = |
Cell Disruption Method | Microfluidizer |
Lytic Agent | None |
Pre-Refolding Purification | Washing inclusion body |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Detergent precipitation/sequestration |
Wash Buffer | see protocol |
Solubilization Buffer | 100 mM Tris-Cl, pH 9.0, 2% (w/v) LDS, 12.5 % (w/v) sucrose |
Refolding Buffer | see protocol |
Pre-Refolding Purification | Washing inclusion body |
Tag Cleaved | no |
Refolding pH | 9.0 |
Refolding Temperature | 4.0 |
Protein Concentration | 0.35 mg/ml |
Refolding Time | 20 min |
Redox Agent | Beta-mercaptoethanol |
Redox Agent Concentration | n/a |
Refolding Protocol | Folding of LHC-II monomers: • heat 0.7 mg inclusion bodies in 1.4 ml Reaction Buffer ( 100 mM Tris-Cl, pH 9.0, 2% (w/v) LDS, 12.5 % (w/v) sucrose) for 5 min at 95ºC • cool to room temperature (~ 15 min) • add 0.15 ml beta-mercaptoethanol (100 mM) • cool on ice. • inject photosynthetic Pigments (0.5 mg Chla/Chlb~3, and 0.15 mg Carotenoids in 0.15 ml EtOH) mix immediately • keep on ice 20 min • add 0.15 ml 10 % (w/v) beta-octyl-glucoside and mix • add 0.2 ml of 3M KCl to precipitate the Dodecylsulfate • keep 10 min on ice. • spin down 5 min maxspeed tabletop • the supernatant is now light green and contains the LHC-II monomers you can easily scale up to a final volume of 150 ml. Folded monomers can be stored at –20° C. for later use Trimerformation on a Ni chelating column • prepare small columns with 1ml chelating Sepharose (Pharmacia) • wash with some water • load 1 ml o.3M NiCl2 • wash with 3 ml ml 50mM Tris pH 7.5 • load folded LHC-II monomers • wash with 1 ml OG buffer (1% (w/v) beta-octyl-glucoside, 0.1 M Tris pH 9.0, 12.5% (w/v) sucrose) • wash with 1 ml TX buffer (0.05% (v/v) Triton X-100, 0.1 mg/ml L-phosphatidyl-D,L-glycerol dipalmitoyl (PG), 0.1 M Tris pH 7.5) • wash with Elution buffer (0.1% (w/v) beta-dodecyl-maltoside, 0.3 M Imidazol pH 7.5) until green fraction starts eluting (about 0.6ml) • elute green fraction with another 1.2 ml Elution buffer the eluted green fraction contains a mixture of refolded LHC-II monomers and trimers with some free pigments Sucrose gradient centrifugation to separate monomers, trimers and free pigments • freeze sucrose solution (20.5% (w/v) sucrose, 50 mM Tris 7.5, 0.05% (w/v) beta-dodecyl-maltoside) in SW40 Ti rotor tubes • thaw sucrose solution slowly at 4° C. • load folded LHC-II • centrifuge overnight in SW40 Ti rotor (20h, 40000 rpm, 200000 g, 4° C.) • use a syringe to harvest trimers (lowest of the three bands) • store protein at –20° C. Good luck and have fun |
Refolding Assay | Fluorescence |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | NULL |
Refolding Yield | 5-10% |
Purity | > 90% |
Notes |