2018
Reduced Occupancy of the Oxygen-Evolving Complex of Photosystem II Detected in Cryo-Electron Microscopy Maps
Wang J, Reiss K, Brudvig GW, Batista VS. Reduced Occupancy of the Oxygen-Evolving Complex of Photosystem II Detected in Cryo-Electron Microscopy Maps. Biochemistry 2018, 57: 5925-5929. PMID: 30260634, DOI: 10.1021/acs.biochem.8b00609.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexElectrostatic potentialOEC of PSIIPhotosystem IIAtomic scattering factorsElectron scatteringScattering factorsDensity functional theoryESP mapsFunctional theoryAtomic coordinatesAtomistic modelMicroscopy mapsScatteringCryo-electron microscopy mapComputational simulationsIdentification of ions in experimental electrostatic potential maps
Wang J, Liu Z, Frank J, Moore PB. Identification of ions in experimental electrostatic potential maps. IUCrJ 2018, 5: 375-381. PMID: 30002838, PMCID: PMC6038950, DOI: 10.1107/s2052252518006292.Peer-Reviewed Original ResearchElectrostatic potentialElectrostatic potential mapsCation-anion pairsX-ray crystallographyCation peaksIonic pairsAtomic chargesAnion peaksIdentification of ionsIsolated ionsAnionsCationsIonsESP valuesAtomsCryo-electron microscopyPotential mapsHigh scattering anglesElectron distributionMacromoleculesChargeUncharged atomsCryo-EM mapsCrystallography
2017
Determination of chemical identity and occupancy from experimental density maps
Wang J. Determination of chemical identity and occupancy from experimental density maps. Protein Science 2017, 27: 411-420. PMID: 29027293, PMCID: PMC5775170, DOI: 10.1002/pro.3325.Peer-Reviewed Original ResearchConceptsCharge densityFourier transformElectrostatic potentialExperimental charge densitySolvent moleculesAtomic B-factorsElectron densityBasic electronic propertiesESP mapsProtein α-helixChemical identityActive siteElectronic propertiesLarge macromolecular complexesExperimental density mapsDensity mapsMoleculesVitreous iceMacromolecular complexesΑ-helixSmall protein subunitESP valuesTransformStructure factorSupercomplexesEffects of aligned α‐helix peptide dipoles on experimental electrostatic potentials
Wang J, Videla PE, Batista VS. Effects of aligned α‐helix peptide dipoles on experimental electrostatic potentials. Protein Science 2017, 26: 1692-1697. PMID: 28556371, PMCID: PMC5563131, DOI: 10.1002/pro.3204.Peer-Reviewed Original ResearchConceptsElectrostatic potentialEM mapsProtein αExperimental electrostatic potentialHelix dipoleDetailed molecular levelHigh-resolution electron microscopyDensity functional theory calculationsProtein functionStructural biologyFunctional theory calculationsElectron microscopyProtein α-helixPartial atomic chargesElectric fieldΑ-helixLong-range featuresMolecular levelNonlocal natureAtomic chargesTheory calculationsDipoleBackbone dipolesRecent breakthroughsProper calculation