A novel protein refolding protocol for the solubilization and purification of recombinant peptidoglycan-associated lipoprotein from Xylella fastidiosa overexpressed in Escherichia coli

► We developed a promising protein refolding protocol for an outer membrane protein. ► The protocol was effective for the solubilization and purification of XfPal. ► High yield of purified protein with secondary and tertiary structure was obtained. ► The refolded XfPal was able to interact in vitro with peptidoglycan. ► This protocol is valuable for future structural and functional studies of XfPal.