Reply to Sleutel and Remaut, “ Structural insights into Escherichia coli CsgA amyloid fibril assembly revisited”

_The _our discovery _{understanding} of functional _{of the} amyloids _Escherichia in _coli bacteria _curli dates _biogenesis back several _system decades, _{has steadily} and evolved over time. Since Chapman’s seminal work in 2002, which involved isolation, characterization, and depolymerization of the major curli subunit CsgA, a variety of structural tools have been employed to elucidate curli architecture. Notably, later on, both solid-state nuclear magnetic resonance spectroscopy (NMR) and X-ray diffraction offered critical insights into the structure of E. coli CsgA fibrils, revealing their hallmark cross-β architecture (1, 2). Despite these advances, curli fibers have remained challenging to characterize structurally, primarily due to the high aggregation propensity and intrinsically disordered nature of monomeric CsgA.