2024
Composition Heterogeneity of Metal Ions Bound at the Oxygen-Evolving Center of Photosystem II in Living Cells
Wang J. Composition Heterogeneity of Metal Ions Bound at the Oxygen-Evolving Center of Photosystem II in Living Cells. Biochemistry 2024, 63: 1963-1968. PMID: 39037205, DOI: 10.1021/acs.biochem.4c00261.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyMetalsModels, MolecularOxygenPhotosystem II Protein ComplexThermosynechococcusConceptsX-ray free-electron lasersStructure of photosystem IIOxygen-evolving centerPhotosystem IICrystal structure of photosystem IIFree-electron laserPhotosystem II dimersPhotosystem ILight-harvesting complexesCryo-electron tomographyMetal ionsPSII samplesCryo-electron microscopyCryo-ETDimeric core complexesCryo-EMMetal ion cofactorsLiving cellsCrystal structureCryo-electronCryo-EM structureMetal-ion occupancyIon occupancySpectroscopic interpretationAsymmetric environment
2022
How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM
Wang J, Liu J, Gisriel CJ, Wu S, Maschietto F, Flesher DA, Lolis E, Lisi GP, Brudvig GW, Xiong Y, Batista VS. How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM. Journal Of Structural Biology 2022, 214: 107902. PMID: 36202310, PMCID: PMC10226527, DOI: 10.1016/j.jsb.2022.107902.Peer-Reviewed Original ResearchConceptsCryo-EM mapsAmino acid residuesAcid residuesCryo-electron microscopy mapIndividual amino acid residuesCyanobacteria Synechocystis spPCC 6803Synechocystis spMicroscopy mapsThermosynechococcus elongatusSARS-CoV-2 spike proteinLocal structural changesResiduesSpike proteinAtomic coordinatesElongatusSubunitsSpeciesProteinSpSimilar structureStructural changes
2021
High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803
Gisriel CJ, Wang J, Liu J, Flesher DA, Reiss KM, Huang HL, Yang KR, Armstrong WH, Gunner MR, Batista VS, Debus RJ, Brudvig GW. High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 119: e2116765118. PMID: 34937700, PMCID: PMC8740770, DOI: 10.1073/pnas.2116765118.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyPhotosystem II Protein ComplexProtein ConformationSynechocystisConceptsCryo-electron microscopy structurePCC 6803Photosystem IIWater oxidationMicroscopy structureMesophilic cyanobacteriumHigh-resolution cryo-electron microscopy structuresOxygen-evolving photosystem IILight-driven water oxidationCyanobacterial photosystem IIHigh-resolution structuresD1 subunitPSII structureSynechocystis spLarge water channelsGenetic manipulationC-terminusBiophysical dataActive siteCyanobacteriumSpStructural pictureSubunitsOxidationWater channelsIdentification of Mg2+ ions next to nucleotides in cryo‐EM maps using electrostatic potential maps
Wang J, Natchiar SK, Moore PB, Klaholz BP. Identification of Mg2+ ions next to nucleotides in cryo‐EM maps using electrostatic potential maps. Acta Crystallographica Section D, Structural Biology 2021, 77: 534-539. PMID: 33825713, PMCID: PMC8025889, DOI: 10.1107/s2059798321001893.Peer-Reviewed Original ResearchMeSH KeywordsCryoelectron MicroscopyCrystallography, X-RayHumansIonsMacromolecular SubstancesModels, MolecularNucleotidesRibosomes
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 simulations
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 factorSupercomplexesExperimental charge density from electron microscopic maps
Wang J. Experimental charge density from electron microscopic maps. Protein Science 2017, 26: 1619-1626. PMID: 28543856, PMCID: PMC5521614, DOI: 10.1002/pro.3198.Peer-Reviewed Original Research
2016
On the interpretation of electron microscopic maps of biological macromolecules
Wang J, Moore PB. On the interpretation of electron microscopic maps of biological macromolecules. Protein Science 2016, 26: 122-129. PMID: 27706888, PMCID: PMC5192980, DOI: 10.1002/pro.3060.Peer-Reviewed Original Research