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The β-barrel assembly machinery (BAM) consisting of the central β-barrel BamA and four other lipoproteins mediates folding of majority of the outer membrane proteins. BamA is placed in an asymmetric bilayer and its lateral gate is suggested to be the functional hotspot. Here we used in situ pulsed electron-electron double resonance spectroscopy to characterize BamA in the native outer membrane. In the detergent micelles, the data is consistent with mainly an inward-open conformation of BamA.doi:10.1002/anie.202113448 pmid:34761852 pmcid:PMC9299766 fatcat:yh26gfcjrjdp5oa62ufpvo2yd4