<p>The goal of this project is to express both the normal CYP26 B1 and the spliced CYP26 B1 from human in <em>Escherichia coli </em>(E.coli) cells for further crystallization. This will be achieved by cloning in the DNA fragments into the Champion pET SUMO vector that is later transformed into <em>E.coli </em>cells. The CYP26 B1 contains a hydrophobic helix at the N-terminal of the protein, making both protein expression and crystallization difficult. Two variants of both full-length CYP26 B1 and the spliced variant will therefore be made, one with the trans-membrane helix present and one without the helix. The SUMO-vector will produce a fusion protein that will make CYP26 B1 more hydrophilic and improve the purification of the two proteins.</p>
| Identifer | oai:union.ndltd.org:UPSALLA/oai:DiVA.org:oru-7394 |
| Date | January 2009 |
| Creators | Sundin, Johanna |
| Publisher | Örebro University, School of Science and Technology |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Student thesis, text |
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