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dc.contributor.authorMcMahon, Stephen
dc.contributor.authorWalsh, MA
dc.contributor.authorChing, RTY
dc.contributor.authorCarter, Lester
dc.contributor.authorDorward, M
dc.contributor.authorJohnson, Kenneth Alan
dc.contributor.authorLiu, Huanting
dc.contributor.authorOke, Muse
dc.contributor.authorBlock Jr, C
dc.contributor.authorKennedy, MW
dc.contributor.authorLatiff, AA
dc.contributor.authorCooper, A
dc.contributor.authorTaylor, Garry Lindsay
dc.contributor.authorWhite, Malcolm Frederick
dc.contributor.authorNaismith, James Henderson
dc.date.accessioned2013-03-27T15:31:04Z
dc.date.available2013-03-27T15:31:04Z
dc.date.issued2006-11
dc.identifier.citationMcMahon , S , Walsh , MA , Ching , RTY , Carter , L , Dorward , M , Johnson , K A , Liu , H , Oke , M , Block Jr , C , Kennedy , MW , Latiff , AA , 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 . https://doi.org/10.1107/S1744309106040036en
dc.identifier.issn1744-3091
dc.identifier.otherPURE: 367618
dc.identifier.otherPURE UUID: 11e89212-83e4-4c0b-bd26-8a022a7ad069
dc.identifier.otherWOS: 000241681700017
dc.identifier.otherScopus: 33750576063
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136132
dc.identifier.otherORCID: /0000-0001-9486-566X/work/60428052
dc.identifier.urihttps://hdl.handle.net/10023/3437
dc.description.abstractRanasmurfin, 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.
dc.format.extent3
dc.language.isoeng
dc.relation.ispartofActa Crystallographica. Section F, Structural biology and crystallization communicationsen
dc.rightsCopyright © 2006 International Union of Crystallographyen
dc.subjectQH426 Geneticsen
dc.subject.lccQH426en
dc.titleCrystallization of Ranasmurfin, a blue coloured protein from Polypedates leucomystaxen
dc.typeJournal articleen
dc.contributor.sponsorBBSRCen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1107/S1744309106040036
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=33750576063&partnerID=8YFLogxKen
dc.identifier.urlhttp://ukpmc.ac.uk/abstract/MED/17077494en
dc.identifier.grantnumberBBS/B/14426en


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