Hi Mohamed, I don't recall such a case of a crystallized proteolytically cleaved contaminant (see our recent summary of contamination cases http://scripts.iucr.org/cgi-bin/paper?ei5009 , and references therein). I would certainly recommend depositing the data at the PDB - it may help others address questions that need the higher resolution, or facilitate MR. We can then also include your protein into our ContaMiner & ContaBase webserver & database. https://strube.cbrc.kaust.edu.sa/contaminer/ Best wishes Stefan
On 5 April 2017 at 00:16, Mohamed Noor <mohamed.n...@staffmail.ul.ie> wrote: > During the crystallization of a totally unrelated protein from a different > bacterium in E. coli, we managed to somehow crystallize an E. coli protein. > It turned out to be only the catalytic domain of an enzyme. Two previous > reports both used recombinant expression of this enzyme followed by limited > proteolysis in order to crystallize this domain. > > Has something like this been reported before? I know the stories of AcrB > etc., but I am looking specifically for a 'naturally proteolyzed' > crystallization. > > Looking at our structure and the previously published one, there is not > much difference, with an rmsd of about 0.3 A but our data resolution is a > bit higher. This is perhaps unsurprising as the unit cells are very similar > (in fact, I just did a quick RBR). Should we bother depositing and > publishing this observation? > > Thanks. > Mohamed >
