The high-resolution structure of the extracellular domain of human CD69 using a novel polymer.
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.
Kolenko
Petr
P
Institute of Macromolecular Chemistry AS CR, v.v.i., Heyrovského nám. 2/1888, 162 06 Praha 6, Czech Republic. kolenko@imc.cas.cz
Skálová
Tereza
T
Vanek
Ondrej
O
Stepánková
Andrea
A
Dusková
Jarmila
J
Hasek
Jindrich
J
Bezouska
Karel
K
Dohnálek
Jan
J
D015703:Antigens, CD / Q000737:chemistry*; D000945:Antigens, Differentiation, T-Lymphocyte / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D037181:Lectins, C-Type / Q000737:chemistry*; D008958:Models, Molecular; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D000099192:CD69 Antigens
D015703:Antigens, CD; D000945:Antigens, Differentiation, T-Lymphocyte; D037181:Lectins, C-Type; D011108:Polymers; D011994:Recombinant Proteins; D000099192:CD69 Antigens