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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

Perzistentní odkaz   https://www.medvik.cz/link/bmc12006554
E-zdroje

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

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 The high-resolution structure of the extracellular domain of human CD69 using a novel polymer / $c P. Kolenko, T. Skálová, O. Vaněk, A. Štěpánková, J. Dušková, J. Hašek, K. Bezouška, .J Dohnálek
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$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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$a CD antigeny $x chemie $7 D015703
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