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Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE

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Albrecht,  R
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Zeth,  K
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Albrecht, R., & Zeth, K. (2010). Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(12), 1586-1590. doi:10.1107/S1744309110034160.


Cite as: https://hdl.handle.net/21.11116/0000-000A-E73C-F
Abstract
In Escherichia coli, the β-barrel assembly machinery (or BAM complex) mediates the recognition, insertion and assembly of outer membrane proteins. The complex consists of the integral membrane protein BamA (an Omp85-family member) and the lipoproteins BamB, BamC, BamD and BamE. The purification and crystallization of BamC, BamD and BamE, each lacking the N-terminal membrane anchor, is described. While the smallest protein BamE yielded crystals under conventional conditions, BamD only crystallized after stabilization with urea. Full-length BamC did not crystallize, but was cleaved by subtilisin into two domains which were subsequently crystallized independently. High-resolution data were acquired from all proteins.