© 2014 International Union of Crystallography. All rights reserved.This study examines the binding and chemical stability of the platinum hexahalides K2PtCl6, K2PtBr6and K2PtI6when soaked into pre-grown hen egg-white lysozyme (HEWL) crystals as the protein host. Direct comparison of the iodo complex with the chloro and bromo complexes shows that the iodo complex is partly chemically transformed to a square-planar PtI3 complex bound to the Nδatom of His15, a chemical behaviour that is not exhibited by the chloro or bromo complexes. Each complex does, however, bind to HEWL in its octahedral form either at one site (PtI6) or at two sites (PtBr6and PtCl6). As heavy-atom derivatives of a protein, the octahedral shape of the hexahalides could be helpful in cases of difficult-to-interpret electron-density maps as they would be recognisable 'objects'.
|Number of pages||2|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - 29 Aug 2014|
- hen egg-white lysozyme
- platinum hexahalides
- PtI3ligand bound to histidine
- X-ray lasers