title: Crystallization and preliminary crystallographic data of a Streptomyces scabies extracellular esterase.
abstract: X-ray quality single crystals of an extracellular esterase from pathogenic Streptomyces scabies were obtained by the hanging drop method. The crystals are monoclinic (space group C2, a = 161.1 A, b = 51.2 A, c = 124.2 A, beta = 100.6 degrees) with two molecules related by a noncrystallographic dyad in the asymmetric unit, with a solvent content of approximately 64%. The diffraction pattern from fresh crystals extends beyond 2 A resolution using sealed tube CuK alpha radiation. The study has been initiated in order to elucidate the mechanism of this unusual non-serine-dependent esterase, and to gain better understanding of the molecular basis of the pathogenesis of the scab disease.
authors.affiliation: Department of Biochemistry, University of Alberta, Edmonton, Canada.
authors.forename: R
authors.initials: R
authors.lastname: Green
authors.forename: J L
authors.initials: JL
authors.lastname: Schottel
authors.forename: L
authors.initials: L
authors.lastname: Swenson
authors.forename: Y
authors.initials: Y
authors.lastname: Wei
authors.forename: Z S
authors.initials: ZS
authors.lastname: Derewenda
mesh_terms: D003460:Crystallization; D004950:Esterases / Q000737:chemistry*; D007091:Image Processing, Computer-Assisted; D011487:Protein Conformation; D013302:Streptomyces / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D004950:Esterases