This may seem an interesting case, given that protocol fur purification, and subsequent crystallization is reproducible as well as this enzyme is a valid drug target for pathogenic strains of E. coli.
Best Z On Apr 5, 2017 02:51, "Vipul Panchal" <panchal.vi...@igib.in> wrote: > I don't think it is going to be any scientific story. Even if you think of > publishing what aspect are you going to discuss? What new are you going to > give to the community. > > On Wed, Apr 5, 2017 at 2:46 AM, 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 >> > > > > -- > Vipul Panchal > Senior Research Fellow, > Respiratory disease and biology, > CSIR-IGIB > (M)-9540113372 >
