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The high-resolution structure of the extracellular domain of human CD69 using a novel polymer.

ABSTRACT: 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.

SUBMITTER: Kolenko P

PROVIDER: S-EPMC2802874 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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The high-resolution structure of the extracellular domain of human CD69 using a novel polymer.

Kolenko Petr P Skálová Tereza T Vanek Ondrej O Stepánková Andrea A Dusková Jarmila J Hasek Jindrich J Bezouska Karel K Dohnálek Jan J

Acta crystallographica. Section F, Structural biology and crystallization communications 20091127 Pt 12

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. ...[more]

PMID: 20054122

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