Difference between revisions of "Team:Uppsala/Medals"

      

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             <li>Register and attend: <br>Our team has been part of the iGEM competition and had an amazing summer developing our Crafting Crocin project. 13 members of our team are registered to attend the Giant Jamboree in Boston and could not be more excited about it.</li>

             <li>Deliverables: <br>We have completed and submitted all 8 required deliverables on time.</li>

         <li>Attribution: <br>We have many people and institution we are thankful for this year. Special thank you belongs of course to our university that provided us with finances and space to do our project. But the many other we want to thank to you can find in our <a href="https://2017.igem.org/Team:Uppsala/Attributions"> Attribution page.</a> </li>

         <li> Characterization/Contribution: <br> This year our team decided to both participate in <a href="https://2017.igem.org/Team:Uppsala/InterLab">Interlab Measument Study </a>. We also decided to characterize an existing <a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K323122">biobrick </a> from 2011 Slovenia team  which has been an inspiration and base to our project. You can read more about the characterization in the <a href="https://2017.igem.org/Team:Uppsala/Zea-Strain">Zeaxanthin</a> page of our project.</li>

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     <li>Validated part: <br>Base of our project was introduction of three enzymes into E. Coli. We validated X (depends on Siri and Oscar) (Biobrick numbers in brackets) of our enzymes via activity assay, XY via sequencing and XY via SDS page.</li>

     <li>Collaboration: <br> Our team takes pride in collaborating with other teams and getting insight from the iGEM community. This year our most notable collaboration was a panel discussion we organized with iGEM Stockholm where more than 100 people participated. But we also worked with iGEM Lund to help them with their first year, organized webinars, made postcard and more! You can read about our collaborations on our Collaboration page. </li>

     <li>Human Practices: <br>This year we decided to focus most of our Human Practice part on ethics in science. We developed something our team calls The Ethics Package. In this we went first to experts to discuss ethical issues of our project, then we talked to the iGEM community in our webinars and lastly we reached out to general public in our panel discussion. Out of all these parts and own our research we compiled Ethical guidelines for iGEM teams with a list of questions that every iGEM team should answer to ethically asses their project. You can read more about our Ethics Package in our Ethics page.</li>

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     <li>Integrated Human Practices: <br>We have already mentioned our Ethics package that you can find at our Ethics page. Then we just needed to put our package to practice. We have done that in the project selection part where we looked at different ethical aspects of our project ideas and decided accordingly. You can read about this on our Human Practice page.</li>

     <li>Improve a previous Part or Project: <br> This year we were working with several parts from previous iGEM projects. Most notably with Zeaxanthine strain from Slovenia 2011 (BBa_K323122). We decided that the production was too unstable in such a large plasmid and adding more steps to it would be too risky. Therefore, we used lambda red recombeenering to add the parts onto chromosome. You can read more about this part of the project at the Zeaxanthine page. <br>Another improvement to previous project is a biorbrick BBa_K2423002 which is an improved version of BBa_K1033112 developed by iGEM Uppsala 2013. We decided to optimize codons in the birobrick, add his tag linker to ensure proper folding and easier purification and to add two stop codons to make transcription smoother and more effective.</li>

     <li>Model your project: <br>One of the largest applications came from homology modelling. Our team was working with poorly characterized proteins with no structures. Our aim was to purify proteins on chromatography column which is also depended on the shape of the protein. Therefore, we made homology models of our proteins to help optimize the purification process. We have also gained insight onto the fact that one of our proteins was working most likely as a tetramer which we needed to address during purification and activity testing. The other thing we adjusted was a position of his-tag for purification as we discovered that the terminal part of one of our protein is most likely buried in the folded protein. You can read more about this and our measurements of Km and Kcat of the proteins on our modelling</li>

     <li>Demonstrate your work:</li>