Stony Brook Team was one of the teams, who worked with the same strain of cyanobacteria Synechococcus elongatus PCC 7942. Collaboration with this team was very helpful for our team since the team shared their protocol of transforming cyanobacteria. At that moment, we troubleshooted the transformation protocol, media plate preparation protocols and antibiotic resistance for obtaining separate single colonies of transformed Synechococcus elongatus. The protocol of Stony Brook Team appeared to be successful and gave us first separate colonies which we could further use for the hydrogen sulfide assay. We, in turn, suggested some solutions for the adjustment of proper temperature for cyanobacteria in their CO2 incubator.

In the frames of collaboration with USP - EEL Brazil iGEM Team, we created a homology model for their expressed protein laccase, which functions to degrade water contaminating estrogens. We found that the homologous protein from the organism Myceliophthora thermophila has a higher affinity binding to 17A-ethinylestradiol than to estrone. Using the protein-ligand docking software, we hypothesized the explanations for the phenomenon in the hydrogen bond in the structure of laccase enzyme, which facilitates the redox reaction in the active site for 17A-ethinylestradiol better than for estrone. Thus, the model showed the affinity of the homologous to laccase from Pleurotus ostreatus protein to two similar ligands and it explained the reasons of difference between the interactions.