title: Crystallization and preliminary crystallographic studies of Streptococcus pyogenes cysteine protease precursor.
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.
authors.affiliation: Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Grunwaldzka 6, 60-780 Poznan, Poland.
authors.forename: Robert
authors.initials: R
authors.lastname: Janowski
authors.forename: Grzegorz
authors.initials: G
authors.lastname: Bujacz
authors.forename: Dieter
authors.initials: D
authors.lastname: Gerlach
authors.forename: Mariusz
authors.initials: M
authors.lastname: Jaskolski
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D008958:Models, Molecular; D013297:Streptococcus pyogenes / Q000737:chemistry*
chemical_list: D003546:Cysteine Endopeptidases