2026· Methods in molecular biology· Vol 3020, pp.
161-172
· 0 citations
Medicine
TL;DR
This chapter outlines a detailed workflow for the expression, purification, and structural analysis of the ABC transporter MsbA from Pseudomonas aeruginosa (PaMsbA), which exemplifies how biochemical optimization, native mass spectrometry, and cryo-electron microscopy (cryo-EM) can be integrated to investigate membrane protein function and structure.
Together, the methods described here demonstrate that careful selection via thorough screening, and optimization of expression and purification conditions, are an invaluable investment of time, ultimately yielding the best target not only for successful high-resolution structural analyses-X-ray crystallography and cryo...
B. Kloss, C. Ardiccioni, V. Petrou et al.· Methods in molecular biology· 0 citations
A generalizable workflow for producing soluble receptor domains from membrane proteins is established and validated HasR constructs suitable for downstream ligand-screening applications, including aptamer and nanobody discovery.
Federico Bosetto, Maria Zacharopoulou, M. Bycroft et al.· bioRxiv· 0 citations
The current protocol outlines a method for membrane purification utilizing ultracentrifugation and detergents, which facilitates the isolation of membrane proteins in their native conformational state.
A. Anjali, W. A. Khan, A. Arockiasamy et al.· Methods in molecular biology· 0 citations
It is shown that the Escherichia coli DedA protein YqjA exists predominantly as a dimer and, by combining structural modelling with site-specific cysteine crosslinking, the most likely dimer interface is identified, which supports a role for lipid binding in the activity of YqjA.
Thomas J. Paige, Jun-Xi Chen, Aline le Roy et al.· bioRxiv· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.