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  • Title: Crystallization and preliminary X-ray crystallographic studies of the plant aspartic proteinase cardosin A.
    Author: Bento I, Frazão C, Coelho R, Wilson K, Dauter Z, Carrondo MA.
    Journal: Acta Crystallogr D Biol Crystallogr; 1998 Sep 01; 54(Pt 5):991-3. PubMed ID: 9757116.
    Abstract:
    The plant aspartic proteinase cardosin A was crystallized using vapour diffusion. Crystals belong to the monoclinic space group C2, cell dimensions a = 116.9 (2), b = 87.2 (8), c = 81.3 (1) A, beta = 104.4 (4) degrees, and contain two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Diffraction data were collected at room temperature with radiation from a synchrotron source up to 2.85 A resolution. When the crystals were flash cooled to 110 K in a nitrogen stream the same resolution limit could also be obtained on a rotating-anode source. Recently, synchrotron radiation together with flash cooling led to an improvement of the diffraction data to 1.72 A resolution.
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