Abstract
Proteinase A from Aspergillus niger var. macrosporus is a non-pepsin-type acid proteinase distinctly different in various properties from the family of pepsin-type aspartic proteinases, and so far it remains unknown which residues participate in the catalysis of the enzyme and how the mechanism operates. The acid proteinase A was crystallized from an ammonium sulfate solution by the hanging-drop vapor diffusion method. The space group of the crystals was P2 12 12 1 with unit cell dimensions of a = 54·7 A ̊ , b = 70·4 A ̊ and c = 38·0 A ̊ . On the assumption that there is one enzyme molecule in the asymmetric unit, the calculated ratio of volume to unit protein mass ( V m) was 1·64 Å 3 per dalton. Diffraction data were collected up to a resolution higher than 1·5 Å, using the Weissenberg camera for macromolecular crystallography with synchrotron radiation. The crystal of proteinase A is, therefore, suitable for the structural analysis with a high resolution.
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