X-ray density can capture alternate conformations of proteins and their ligands

Summary

X-ray-crystallography density can capture alternate conformations of proteins and their ligands (1). These conformations can often be stably modeled with molecular dynamics.

See also

• Structure ensemble prediction methods are unable to accurately model subtle conformational differences captured by X-ray crystallography

1.

Rosenberg AA, Vedula S, Bronstein AM, Marx A. Seeing Double: Molecular dynamics simulations reveal the stability of certain alternate protein conformations in crystal structures. openRxiv; 2024. Available from: https://doi.org/10.1101/2024.08.31.610605