It looks pretty metallic. It would be good to know the max peak height in rms for the difference map and also some of the distances between the His and Cys side chains. Are your sulphur occupancies alright ;-?
On 21 Jan 2020 17:55, Chris Fage <[email protected]> wrote:
Dear CCP4BB Users,I've recently solved the ~2.2 angstrom structure of a protein. In my electron density there are unusual monomer-monomer interfaces involving pairs of His and Cys residues (see https://ibb.co/wdWBcdk). Note the positive Fo-Fc density between the four side chains. As there is not adequate space for a water molecule or metal ion, perhaps the Cys residues are partially tied up disulfide bonds? However, the protein looks to be fully monomeric based on LC-MS measurements. Has anyone else observed crystal-driven formation of disulfide bridges?Aside from this region, there is no extensive interface between momoners, and PDBePISA suggests a monomeric state.Thanks in advance for any advice!Best wishes,Chris
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