Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
19193998
PubMed Central
PMC2635868
DOI
10.1107/s1744309108040578
PII: S1744309108040578
Knihovny.cz E-zdroje
- MeSH
- fotosystém II (proteinový komplex) analýza chemie MeSH
- krystalizace MeSH
- krystalografie rentgenová MeSH
- rekombinantní proteiny analýza chemie MeSH
- rostlinné proteiny analýza chemie MeSH
- Spinacia oleracea chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- fotosystém II (proteinový komplex) MeSH
- rekombinantní proteiny MeSH
- rostlinné proteiny MeSH
Preliminary X-ray diffraction analysis of the extrinsic PsbP protein of photosystem II from spinach (Spinacia oleracea) was performed using N-terminally His-tagged recombinant PsbP protein overexpressed in Escherichia coli. Recombinant PsbP protein (thrombin-digested recombinant His-tagged PsbP) stored in bis-Tris buffer pH 6.00 was crystallized using the sitting-drop vapour-diffusion technique with PEG 550 MME as a precipitant and zinc sulfate as an additive. SDS-PAGE analysis of a dissolved crystal showed that the crystals did not contain the degradation products of recombinant PsbP protein. PsbP crystals diffracted to 2.06 A resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 38.68, b = 46.73, c = 88.9 A.
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Resonance assignment of PsbP: an extrinsic protein from photosystem II of Spinacia oleracea
