A major secreted aspartic proteinase from Candida albicans has been crystallized in the presence of inhibitors to prevent autodegradation. With pepstatin a cleaved form of the enzyme was nevertheless found in the crystals whereas with the inhibitor A70450 the enzyme remained intact. The crystals containing pepstatin were not suitable for X-ray data collection while the crystals containing A70450 grew by vapour diffusion as tetragonal bipyramids, space group P43212 (or P 41212), a = b = 76·2 Å, c = 126·1 Å, with one molecule in the asymmetric unit and they diffract to beyond 2·2 Å.

An exoglucanase, with specificity for β(1,3) linkages, from the cell wall of Candida albicans has been crystallized by the hanging drop method in the presence of polyethylene glycol 8000. The crystals, which diffract to better than 1.9 Å resolution, belong to the orthorhombic space group P212121 with cell constants a = 60.2 Å, b = 65.2 Å, c = 96.5 Å and with one molecule in the asymmetric unit.