Crystallization of Ranasmurfin, a blue coloured protein from Polypedates leucomystax
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Ranasmurfin, a previously uncharacterized similar to 13 kDa blue protein found in the nests of the frog Polypedates leucomystax, has been purified and crystallized. The crystals are an intense blue colour and diffract to 1.51 angstrom with P2(1) symmetry and unit-cell parameters a = 40.9, b = 59.9, c = 45.0 angstrom, beta = 93.3 degrees. Self-rotation function analysis indicates the presence of a dimer in the asymmetric unit. Biochemical data suggest that the blue colour of the protein is related to dimer formation. Sequence data for the protein are incomplete, but thus far have identified no model for molecular replacement. A fluorescence scan shows a peak at 9.676 keV, indicating that the protein binds zinc and suggesting a route for structure solution.
McMahon , S , Walsh , M A , Ching , R T Y , Carter , L , Dorward , M , Johnson , K A , Liu , H , Oke , M , Block Jr , C , Kennedy , M W , Latiff , A A , Cooper , A , Taylor , G L , White , M F & Naismith , J H 2006 , ' Crystallization of Ranasmurfin, a blue coloured protein from Polypedates leucomystax ' Acta Crystallographica. Section F, Structural biology and crystallization communications , vol 62 , no. Pt 11 , pp. 1124-1126 . DOI: 10.1107/S1744309106040036
Acta Crystallographica. Section F, Structural biology and crystallization communications
Copyright © 2006 International Union of Crystallography
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