Open AccessStructure of the H107R variant of the extracellular domain of mouse NKR‐P1A at 2.3 Å resolution
Author(s) -
Kolenko Petr,
Rozbeský Daniel,
Vaněk Ondřej,
Bezouška Karel,
Hašek Jindřich,
Dohnálek Jan
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111046203
Subject(s) - dimer , resolution (logic) , crystallography , extracellular , crystal twinning , molecule , domain (mathematical analysis) , ion , receptor , diffraction , chemistry , materials science , physics , biochemistry , optics , mathematical analysis , microstructure , mathematics , organic chemistry , artificial intelligence , computer science
The structure of the H107R variant of the extracellular domain of the mouse natural killer cell receptor NKR‐P1A has been determined by X‐ray diffraction at 2.3 Å resolution from a merohedrally twinned crystal. Unlike the structure of the wild‐type receptor in space group I 4 1 22 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I 4 1 with a dimer in the asymmetric unit. Different degrees of merohedral twinning were detected in five data sets collected from different crystals. The mutation does not have a significant impact on the overall structure, but led to the binding of an additional phosphate ion at the interface of the molecules.