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Hen egg white lysozyme (HEWL) co-crystallisation conditions of carboplatinwithout sodium chloride (NaCl) have been utilised to eliminate partialconversion of carboplatin to cisplatin observed previously. Tetragonal HEWLcrystals were successfully obtained in 65% MPD with 0.1M citric acid buffer atpH 4.0 including DMSO. The X-ray diffraction data resolution to be used for themodel refinement was reviewed using several topical criteria together. TheCC1/2 criterion implemented in XDS led to data being significant to 2.0{\AA},compared to the data only being able to be processed to 3.0{\AA} using theBruker software package (SAINT). Then using paired protein model refinementsand DPI values based on the FreeR value, the resolution limit was fine tuned tobe 2.3{\AA}. Interestingly this was compared with results from the EVALsoftware package which gave a resolution limit of 2.2{\AA} solely using<I/sigI> crossing 2, but 2.8{\AA} based on the Rmerge values (60%). Thestructural results showed that carboplatin bound to only the N{\delta} bindingsite of His-15 one week after crystal growth, whereas five weeks after crystalgrowth, two molecules of carboplatin are bound to the His-15 residue. Insummary several new results have emerged: - firstly non-NaCl conditions showeda carboplatin molecule bound to His-15 of HEWL; secondly binding of onemolecule of carboplatin was seen after one week of crystal growth and twomolecules were bound after five weeks of crystal growth; and thirdly the use ofseveral criteria to determine the diffraction resolution limit led to thesuccessful use of data to higher resolution.

Carboplatin binding to a model protein in non-NaCl conditions to  eliminate partial conversion to cisplatin, and the use of different criteria  to choose the resolution limit