Featured Publications
Cryo-EM structure of the insect olfactory receptor Orco
Butterwick JA, del Mármol J, Kim KH, Kahlson MA, Rogow JA, Walz T, Ruta V. Cryo-EM structure of the insect olfactory receptor Orco. Nature 2018, 560: 447-452. PMID: 30111839, PMCID: PMC6129982, DOI: 10.1038/s41586-018-0420-8.Peer-Reviewed Original ResearchConceptsAnchor domainOdorant receptorsSingle-particle cryo-electron microscopy structureCryo-electron microscopy structureMinimal sequence conservationReceptor familyRemarkable sequence diversityCryo-EM structureInter-subunit interactionsMicroscopy structureSequence conservationSequence diversityÅ resolutionCentral poreStructural insightsIon channelsOrcoSuch diversityOlfactory systemDiversityEnormous varietyOdor tuningFamilyInsectsSubunits
2009
Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA
Endeward B, Butterwick JA, MacKinnon R, Prisner TF. Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA. Journal Of The American Chemical Society 2009, 131: 15246-15250. PMID: 19919160, PMCID: PMC2779547, DOI: 10.1021/ja904808n.Peer-Reviewed Original ResearchMeSH KeywordsBacteriaBacterial ProteinsElectron Spin Resonance SpectroscopyElectronsModels, MolecularMutationPotassium ChannelsProtein Structure, QuaternaryProtein Structure, TertiaryConceptsPELDOR dataElectron-electron double resonance measurementsTransverse spin relaxation timeProbe frequencySpin relaxation timeDouble resonance measurementsChannel KcsAMagnetic field strengthSpin-label distancesCentral channel axisPELDOR experimentsDetergent-solubilized samplesField strengthRelaxation timeOscillation frequencyResonance determinationQuantitative simulationChannel axisKcsAFrequencyOrientationMeasurementsAngle