title: Purification, crystallization and preliminary X-ray diffraction analysis of the Staphylococcus epidermidis extracellular serine protease Esp.
abstract: Esp, an extracellular serine protease from Staphylococcus epidermidis, has been shown to inhibit S. aureus biofilm formation and nasal colonization. The full-length 27 kDa pro-Esp was purified and digested with thermolysin to obtain mature Esp. The mature Esp containing 216 residues crystallized in space group P2(1), with unit-cell parameters a = 39.5, b = 61.2, c = 42.5 Å, β = 98.2° and one molecule in the asymmetric unit, with an estimated solvent content of 42%. A diffraction data set has been collected to 1.8 Å resolution on a rotating-anode home-source facility.
authors.affiliation: UNESCO Regional Centre for Biotechnology RCB, Gurgaon, Haryana 122 016, India.
authors.forename: Krishnan
authors.initials: K
authors.lastname: Vengadesan
authors.forename: Kevin
authors.initials: K
authors.lastname: Macon
authors.forename: Shinya
authors.initials: S
authors.lastname: Sugumoto
authors.forename: Yoshimitsu
authors.initials: Y
authors.lastname: Mizunoe
authors.forename: Tadayuki
authors.initials: T
authors.lastname: Iwase
authors.forename: Sthanam V L
authors.initials: SV
authors.lastname: Narayana
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D013212:Staphylococcus epidermidis / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D012697:Serine Endopeptidases