title: Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein.
abstract: Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been overexpressed, purified and crystallized. The protein crystallizes in space group P6(1/5)22, with unit-cell parameters a = b = 157.8, c = 307.3 A. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 A resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of >9 subunits.
authors.affiliation: Centre for Biomolecular Sciences, The University, St Andrews KY16 9ST, Scotland.
authors.forename: Andrew R
authors.initials: AR
authors.lastname: McEwan
authors.forename: Huanting
authors.initials: H
authors.lastname: Liu
authors.forename: Muse
authors.initials: M
authors.lastname: Oke
authors.forename: Lester
authors.initials: L
authors.lastname: Carter
authors.forename: Helen
authors.initials: H
authors.lastname: Powers
authors.forename: Mark
authors.initials: M
authors.lastname: Dorward
authors.forename: Stephen A
authors.initials: SA
authors.lastname: McMahon
authors.forename: Malcolm F
authors.initials: MF
authors.lastname: White
authors.forename: James H
authors.initials: JH
authors.lastname: Naismith
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment; D048229:Sulfolobus solfataricus / Q000737:chemistry*
chemical_list: D019843:Archaeal Proteins