Spatially Separating the Conformers of a Dipeptide.

Atomic-resolution-imaging approaches for single molecules, such as coherent X-ray diffraction at free-electron lasers, require the delivery of high-density beams of identical molecules. However, even very cold beams of biomolecules typically have multiple conformational states populated. We demonstrate the production of very cold (Trot ≈2.3 K) molecular beams of intact dipeptide molecules, which were then spatially separated into the individual populated conformational states. This is achieved using the combination of supersonic expansion laser-desorption vaporization with electrostatic deflection in strong inhomogeneous fields. This represents the first demonstration of a conformer-separated and rotationally cold molecular beam of a peptide, which enables the investigation of conformer-specific chemistry using inherently non-conformer-specific techniques. It furthermore represents a milestone toward the direct structural imaging of individual biological molecules with atomic resolution by ultrafast diffractive-imaging methods.