Abstract
BamA is the central component of the BAM complex and contains a C-terminal β-barrel domain embedded in the outer membrane, and a soluble, periplasmic domain, made out of five polypeptide transport associated (POTRA) motifs. Structural characterization of the POTRA domains was carried out by a combination of crystallographic, NMR and solution Small Angle X-ray Scattering (SAXS) approaches. Despite its limited resolution, SAXS is an excellent complement to NMR and crystallography. It is well suited to validate high-resolution models in solution and is particularly useful to characterize flexible systems such as the POTRA domains of BamA. Here we present a protocol for sample preparation and discuss the considerations of SAXS data collection and quality control, which is applicable to most soluble proteins.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
