Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein.
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.
McEwan
Andrew R
AR
Centre for Biomolecular Sciences, The University, St Andrews KY16 9ST, Scotland.
Liu
Huanting
H
Oke
Muse
M
Carter
Lester
L
Powers
Helen
H
Dorward
Mark
M
McMahon
Stephen A
SA
White
Malcolm F
MF
Naismith
James H
JH
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*
D019843:Archaeal Proteins