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Purification and Bicelle Crystallization for Structure Determination of the E. coli Outer Membrane Protein TamA

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)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article
Article Subtype:Research Article
Bibsysno:Link to catalogue
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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Last Modified:25 Jun 2018 11:47
Deposited On:06 Nov 2015 10:21

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