McMahon Stephen A, Walsh Martin A, Ching Rosalind Tan Yan, Carter Lester G, Dorward Mark, Johnson Kenneth A, Liu Huanting, Oke Muse, Bloch Carlos, Kennedy Malcolm W, Latiff Aishah A, Cooper Alan, Taylor Garry L, White Malcolm F, Naismith James H
Centre for Biomolecular Science and The Scottish Structural Proteomics Facility, The University of St Andrews Fife KY16 9RH, Scotland, UK.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1124-6. doi: 10.1107/S1744309106040036. Epub 2006 Oct 20.
Ranasmurfin, a previously uncharacterized approximately 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 A with P2(1) symmetry and unit-cell parameters a = 40.9, b = 59.9, c = 45.0 A, 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.