The crystal structure of crambin, a 46‐residue protein containing the equivalent of approximately 400 fully occupied non‐H‐atom positions, was originally solved at 1.5 Å by exploiting the anomalous scattering of its six S atoms at a single wavelength far removed from the absorption edge of sulfur. The crambin structure has now been resolved without the use of any anomalous‐dispersion measurements. The technique employed was anab initio`shake‐and‐bake' method, consisting of a phase‐refinement procedure based on the minimal function alternated with Fourier refinement. This method has successfully yielded solutions for a smaller molecule (28 atoms) using 1.2 Å data, and a crambin solution wa