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  • Title: Crystallization and preliminary crystallographic studies of Streptococcus pyogenes cysteine protease precursor.
    Author: Janowski R, Bujacz G, Gerlach D, Jaskolski M.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Apr; 58(Pt 4):723-6. PubMed ID: 11914508.
    Abstract:
    Streptococcal protease precursor, secreted by the human pathogen Streptococcus pyogenes, becomes activated to a cysteine protease. The precursor and the mature enzyme appear to contribute to S. pyogenes virulence. The precursor protein was crystallized in the form of very thin flexible flakes. X-ray diffraction data were collected to 3.15 A resolution at 100 K using synchrotron radiation. The crystals are monoclinic, space group P2(1), with unit-cell parameters a = 41.6, b = 136.0, c = 156.7 A, beta = 95.7 degrees, and contain four copies of the protein in the asymmetric unit.
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