Open AccessCrystallization and preliminary X‐ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE
Author(s) -
Albrecht Reinhard,
Zeth Kornelius
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110034160
Subject(s) - crystallization , bama , escherichia coli , membrane , crystallography , subtilisin , membrane protein , chemistry , biology , biophysics , bacterial outer membrane , biochemistry , enzyme , organic chemistry , gene
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.