Integral membrane proteins perform a wide range of biological processes, including respiration, signal transduction and molecular transport. Structural information is necessary for a full understanding of the mechanisms by which integral membrane proteins work. Ferrous iron transporter protein B (FeoB) is an integral membrane protein of Escherichia coli which is considered to transport ferrous iron in to bacteria. But there are no definite proofs or clear indications of the precise mechanism of ferrous transport. By expressing and crystallizing the G-protein domain (FeoGP) and FeoB, it will be helpful to know about the iron transport system. In order to express FeoB and FeoGP, expression vector pFeoB (FeoB in pGEX-4T-1) and pFeoGP (FeoB in pGEX-4T-1) were made. FeoB and FeoGP proteins were expressed and purified. Using vapour diffusion method crystallization trials of FeoB and FeoGP were done. Crystals of FeoGP are observed and no crystal formation for FeoB. Native crystals of FeoGP diffracted to 2.2 ?? resolution, and mant-GMPPNP crystals to 2.6 ??. Preliminary data processing indicate space group P212121 for native crystals, with cell dimensions 46 x 119 x 146 ??. The data set is 100% complete, Rmerge 0.08, and I/ ?? 3.2.
| Identifer | oai:union.ndltd.org:ADTP/257394 |
| Date | January 2007 |
| Creators | Thambiraj, Solomon Rajesh, Physics, Faculty of Science, UNSW |
| Publisher | Awarded by:University of New South Wales. School of Physics |
| Source Sets | Australiasian Digital Theses Program |
| Language | English |
| Detected Language | English |
| Rights | Copyright Solomon Rajesh Thambiraj, http://unsworks.unsw.edu.au/copyright |
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