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Five test structures (orthorhombic and trigonal trypsin, cubic and rhombohedral insulin and thaumatin) have been solved by the SAD (single-wavelength anomalous diffraction) method using highly redundant data collected at 100 K with a CCD detector, rotating-anode generator and three-circle goniometer. The very weak anomalous scattering (primarily from sulfur) was sufficient to locate all the anomalous scatterers using the integrated direct and Patterson methods in SHELXD. These positions and occupancies were used without further refinement to estimate phases that were extended to native (in-house) resolution by the sphere of influence algorithm in SHELXE. The final map correlation coefficients relative to the anisotropically refined structures were in the range 0.81-0.97. The use of highly redundant medium-resolution laboratory data for sulfur-SAD phasing combined with high-resolution synchrotron native data for phase expansion and structure refinement clearly has considerable potential.

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