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The interleukin-2 tyrosine kinase Src homology 2 domain was crystallized and its structure was solved to 2.35 Å resolution. The structure reveals a domain-swapped dimer that is related to other dimeric SH2 domains solved previously. The cistrans-prolyl isomerization that is evident from solution studies of Itk SH2 cannot be observed in the crystal structure.

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The amino-terminal domain of the Hsp70 co-chaperone Bag2 from M. musculus has been crystallized in native and selenomethionyl forms diffracting to 2.27 and 3.1 Å resolution, respectively.
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