The high-resolution structure of the extracellular domain of human CD69 using a novel polymer
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
20054122
PubMed Central
PMC2802874
DOI
10.1107/s1744309109043152
PII: S1744309109043152
Knihovny.cz E-zdroje
- MeSH
- CD antigeny chemie MeSH
- diferenciační antigeny T-lymfocytů chemie MeSH
- konformace proteinů MeSH
- krystalografie rentgenová MeSH
- lektiny typu C chemie MeSH
- lidé MeSH
- molekulární modely MeSH
- polymery chemie MeSH
- rekombinantní proteiny chemie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- CD antigeny MeSH
- CD69 antigen MeSH Prohlížeč
- diferenciační antigeny T-lymfocytů MeSH
- lektiny typu C MeSH
- polymery MeSH
- rekombinantní proteiny MeSH
The structure of the extracellular domain of human CD69 has been determined by single-crystal X-ray diffraction. The structure refined to 1.37 A resolution provides further details of the overall structure and the asymmetric interface between the monomers in the native dimer. The protein was crystallized using di[poly(ethylene glycol)] adipate, which also served as a cryoprotectant. This is the first report of a crystal structure determined using crystals grown with this polymer.
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PDB
3HUP, R3HUPSF