title: Cloning, expression, crystallization and preliminary X-ray analysis of the DNA-binding protein Sso10a from Sulfolobus solfataricus.
abstract: The gene for the DNA-binding protein Sso10a from the hyperthermophilic archaeon Sulfolobus solfataricus was cloned and overexpressed in Escherichia coli. Crystals of the purified protein have been grown that diffract to beyond 2.15 A resolution. The protein crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 57.24, b = 60.16, c = 69.96 A. With one dimer per asymmetric unit, the crystal to volume per protein mass (V(M)) is 2.9 A(3) Da(-1) and the solvent content is approximately 57%. Complete X-ray diffraction native data were collected from a single crystal and processed to 2.15 A.
authors.affiliation: Chemistry Department, University of Alabama in Huntsville, Huntsville, AL 35899, USA. tealem@email.uah.edu
authors.forename: M J
authors.initials: MJ
authors.lastname: Teale
authors.forename: M
authors.initials: M
authors.lastname: Kahsai
authors.forename: S K
authors.initials: SK
authors.lastname: Singh
authors.forename: S P
authors.initials: SP
authors.lastname: Edmondson
authors.forename: R
authors.initials: R
authors.lastname: Gupta
authors.forename: J W
authors.initials: JW
authors.lastname: Shriver
authors.forename: E
authors.initials: E
authors.lastname: Meehan
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D016415:Sequence Alignment; D016944:Sulfolobus / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D019843:Archaeal Proteins; D004268:DNA-Binding Proteins