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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 I4122 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I41 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.

Supporting information

hkl

Structure factor file (CIF format) https://doi.org/10.1107/S1744309111046203/hv52033T3Asup1.hkl
Contains datablock r3t3asf

PDB reference: H107R mNKR-P1A, 3t3a


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