A simple and versatile system for resonance Raman (RR) spectroscopic analysis of enzyme-substrate complexes at liquid helium temperatures is described. The system allows us to record high-quality RR spectra for dithioacyl papain intermediates (MeO-Phe-Gly- and MeO-Gly-Gly-Phe-Gly-C(= S)S-papain) in ice matrices at 5 K. Based on established structure-spectra correlations, it is concluded that the active-site conformation of the intermediates about the phi', psi' glycinic linkages and cysteine-25 side chain is B-G+-P(H) both in ice matrices at 5 K and in solution at room temperature.