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  • Title: Purification, crystallization and preliminary X-ray analysis of mexicain.
    Author: Oliver-Salvador MC, González-Ramírez LA, Gavira JA, Soriano-García M, García-Ruiz JM.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 Nov; 60(Pt 11):2058-60. PubMed ID: 15502326.
    Abstract:
    Mexicain is a 23.7 kDa papain-like cysteine protease from the tropical plant Jacaratia mexicana. Extracted as a mix of proteases from the latex of the fruit, mexicain is isolated after cation-exchange chromatography as the most abundant product. The purified product inhibited with E-64 was crystallized by sitting-drop vapour diffusion in the presence of ethanolamine. Cryoprotected crystals diffracted X-rays from a home source to 1.98 A and belong to the monoclinic space group P2(1), with unit-cell parameters a = 57.36, b = 90.45, c = 80.39 A, beta = 92.64 degrees . The asymmetric unit contains four molecules of mexicain, with a corresponding crystal volume per protein weight (V(M)) of 2.24 A(3) Da(-1) and a solvent content of 45% by volume. A molecular-replacement model has been determined and refinement is in progress.
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