Gruss, Fabian and Hiller, Sebastian and Maier, Timm. (2015) Purification and Bicelle Crystallization for Structure Determination of the E. coli Outer Membrane Protein TamA. Methods in Molecular Biology, 1329. pp. 259-270.
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Official URL: http://edoc.unibas.ch/dok/A6438826
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Abstract
TamA is an Omp85 protein involved in autotransporter assembly in the outer membrane of Escherichia coli. It comprises a C-terminal 16-stranded transmembrane β-barrel as well as three periplasmic POTRA domains, and is a challenging target for structure determination. Here, we present a method for crystal structure determination of TamA, including recombinant expression in E. coli, detergent extraction, chromatographic purification, and bicelle crystallization in combination with seeding. As a result, crystals in space group P21212 are obtained, which diffract to 2.3 Å resolution. This protocol also serves as a template for structure determination of other outer membrane proteins, in particular of the Omp85 family.
| Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller) 05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier) |
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| UniBasel Contributors: | Hiller Odermatt, Sebastian |
| Item Type: | Article |
| Article Subtype: | Research Article |
| Publisher: | Humana Press |
| ISSN: | 1064-3745 |
| e-ISSN: | 1940-6029 |
| Note: | Publication type according to Uni Basel Research Database: Journal article |
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| Identification Number: |
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| Last Modified: | 13 Dec 2017 14:26 |
| Deposited On: | 06 Nov 2015 10:21 |
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