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The high-resolution structure of the extracellular domain of human CD69 using a novel polymer
P. Kolenko, T. Skálová, O. Vaněk, A. Štěpánková, J. Dušková, J. Hašek, K. Bezouška, .J Dohnálek
Jazyk angličtina Země Velká Británie
Typ dokumentu práce podpořená grantem
NLK
Free Medical Journals
od 2005 do 2013
PubMed Central
od 2005 do 2013
Europe PubMed Central
od 2005 do 2013
Wiley Online Library (archiv)
od 2005-01-01 do 2012-12-31
- 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 MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- práce podpořená grantem 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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- $a Kolenko, Petr $7 xx0124748 $u Institute of Macromolecular Chemistry AS CR, v.v.i., Heyrovskeho nam. 2/1888, 162 06 Praha 6, Czech Republic. kolenko@imc.cas.cz
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- $a 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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