title: Crystallization of a Mos1 transposase-inverted-repeat DNA complex: biochemical and preliminary crystallographic analyses.
abstract: A complex formed between Mos1 transposase and its inverted-repeat DNA has been crystallized. The crystals diffract to 3.25 A resolution and exhibit monoclinic (P2(1)) symmetry, with unit-cell parameters a = 120.8, b = 85.1, c = 131.6 A, beta = 99.3 degrees . The X-ray diffraction data display noncrystallographic twofold symmetry and characteristic dsDNA diffraction at approximately 3.3 A. Biochemical analyses confirmed the presence of DNA and full-length protein in the crystals. The relationship between the axis of noncrystallographic symmetry, the unit-cell axes and the DNA diffraction pattern are discussed. The data are consistent with the previously proposed model of the paired-ends complex containing a dimer of the transposase.
authors.affiliation: School of Biological Sciences, University of Edinburgh, The King's Buildings, Mayfield Road, Edinburgh EH9 3JR, Scotland. jrichard@staffmail.ed.ac.uk
authors.forename: Julia M
authors.initials: JM
authors.lastname: Richardson
authors.forename: David J
authors.initials: DJ
authors.lastname: Finnegan
authors.forename: Malcolm D
authors.initials: MD
authors.lastname: Walkinshaw
mesh_terms: D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D009690:Nucleic Acid Conformation; D019895:Transposases / Q000737:chemistry*
chemical_list: D017931:DNA Primers; D004268:DNA-Binding Proteins; C111652:mariner transposases; D019895:Transposases