Team:Berkeley Wetlab

From 2009.igem.org

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<big><font size="5" face="Book Antiqua"> Abstract</font> </big> <br>
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<center> <big><font size="5" face="Book Antiqua">Preliminary project description</font> </big></center>
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Cell surface display in ''E. coli'' tethers proteins to the outer membrane in order to localize them to the extracellular environment.  While this form of localization has allowed many novel functions to be engineered into ''E. coli'', work within this space relies on a trial and error approach rather than design principles. We worked to create a foundation of research which would make the rational design of cell surface display systems in ''E. coli''  possible.  We used a combinatorial approach to compare the ability of different display proteins to display different classes of functional proteins. This required the development and implementation of an automated assembly method able to construct the large number of devices necessary to draw meaningful conclusions about design within this space. 
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The University of California Berkeley iGEM team is proposing to expand the design space of synthetic biology by exploring novel applications of cell surface display within Escherichia coli, the gold standard organism for bacterial engineering. The team envisions a bottom-up design scheme in order to tackle this engineering problem in a well organized, modular fashion. In order to overcome the challenges of engineering Escherichia coli cell surface display, a high throughput, automated, combinatorial strategy is employed to control the system.
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<font size="5" face="Book Antiqua">Acknowledgements:</font> <br>
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<center><font size="5" face="Book Antiqua">Our Team</font></center> <br>
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<font size="5" face="Book Antiqua">Acknowledgements</font> <br>
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We thank our wonderful advisers: Chris Anderson, Terry Johnson, and Lane Weaver for their guidance and support. We also thank our generous sponsors:<br>
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Latest revision as of 19:14, 21 October 2009


Display-o-matic2.png

Abstract
Cell surface display in E. coli tethers proteins to the outer membrane in order to localize them to the extracellular environment. While this form of localization has allowed many novel functions to be engineered into E. coli, work within this space relies on a trial and error approach rather than design principles. We worked to create a foundation of research which would make the rational design of cell surface display systems in E. coli possible. We used a combinatorial approach to compare the ability of different display proteins to display different classes of functional proteins. This required the development and implementation of an automated assembly method able to construct the large number of devices necessary to draw meaningful conclusions about design within this space.




Our Team

BerkeleyWetlabTeam.jpg



Acknowledgements
We thank our wonderful advisers: Chris Anderson, Terry Johnson, and Lane Weaver for their guidance and support. We also thank our generous sponsors:


Berkeleyinvitrogen.jpg Berkeleynsf.jpg Berkeleyqbs.jpg Berkeleysynberg.png