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 channels
2019
Visualization of H atoms in the X‐ray crystal structure of photoactive yellow protein: Does it contain low‐barrier hydrogen bonds?
Wang J. Visualization of H atoms in the X‐ray crystal structure of photoactive yellow protein: Does it contain low‐barrier hydrogen bonds? Protein Science 2019, 28: 1966-1972. PMID: 31441173, PMCID: PMC6798185, DOI: 10.1002/pro.3716.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCrystallography, X-RayHydrogen BondingModels, MolecularPhotoreceptors, MicrobialProtein ConformationConceptsPhotoactive yellow proteinLow-barrier hydrogen bondH atomsYellow proteinResidual electron density mapsNeutron structureAtomsO bond angleO distancesO atomsHydrogen bondsElectron density mapsBond anglesDensity mapsX-ray structureCrystal structureResolution X-ray structureStructureBondsX-ray crystal structureCrystallographic identification of spontaneous oxidation intermediates and products of protein sulfhydryl groups
Wang J. Crystallographic identification of spontaneous oxidation intermediates and products of protein sulfhydryl groups. Protein Science 2019, 28: 472-477. PMID: 30592103, PMCID: PMC6371210, DOI: 10.1002/pro.3568.Peer-Reviewed Original ResearchConceptsLys side chainsSide chainsO bridgesChemical identificationCrystal structureElectron density featuresCross-linking speciesCys side chainDirect chemical identificationProtein crystal structuresMass spectrometric analysisOxidation intermediatesCys-245Primary aminesMethylene groupCrystallographic identificationSpectrometric analysisDehydration mechanismLys-158Protein sulfhydryl groupsSulfhydryl groupsProtein structureChainCHCys residues
2018
On the damage done to the structure of the Thermoplasma acidophilum proteasome by electron radiation
Wang J, Liu Z, Crabtree RH, Frank J, Moore PB. On the damage done to the structure of the Thermoplasma acidophilum proteasome by electron radiation. Protein Science 2018, 27: 2051-2061. PMID: 30242932, PMCID: PMC6237698, DOI: 10.1002/pro.3511.Peer-Reviewed Original ResearchMeSH KeywordsElectronsModels, MolecularProteasome Endopeptidase ComplexProtein ConformationThermoplasmaConceptsLocal chemical effectsElectron beamElectron radiationChemical mechanismStructure effectsChemical effectsElectron microscopeBackbone atomsChemical damageΑ-helixThermoplasma acidophilumMoleculesDose-dependent degradationQuaternary structureElectronsBeamAtomsEM mapsRadiationStructureMicroscopeResolutionSmall changesAcidophilum
2017
Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima
An JY, Sharif H, Kang GB, Park KJ, Lee JG, Lee S, Jin MS, Song JJ, Wang J, Eom SH. Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima. Biochemical And Biophysical Research Communications 2017, 495: 1201-1207. PMID: 29180014, DOI: 10.1016/j.bbrc.2017.11.158.Peer-Reviewed Original ResearchConceptsPeriplasmic domainMisfolded membrane proteinsATP-dependent proteaseMembrane protein complexesResolution crystal structureHydrophobic membrane environmentMembrane homeostasisProtein complexesMembrane proteinsTransmembrane proteinMembrane environmentThermotoga maritimaStructural insightsFtsHProtease domainToxic proteinsProteinOligomerizationHigh energetic barrierDomainTranslocatesEnergetic barrierMaritimaHomeostasisCrystal structure
2016
X‐ray radiation‐induced addition of oxygen atoms to protein residues
Wang J. X‐ray radiation‐induced addition of oxygen atoms to protein residues. Protein Science 2016, 25: 1407-1419. PMID: 27074249, PMCID: PMC4989999, DOI: 10.1002/pro.2934.Peer-Reviewed Original ResearchS3 State of the O2‑Evolving Complex of Photosystem II: Insights from QM/MM, EXAFS, and Femtosecond X‑ray Diffraction
Askerka M, Wang J, Vinyard DJ, Brudvig GW, Batista VS. S3 State of the O2‑Evolving Complex of Photosystem II: Insights from QM/MM, EXAFS, and Femtosecond X‑ray Diffraction. Biochemistry 2016, 55: 981-984. PMID: 26849148, DOI: 10.1021/acs.biochem.6b00041.Peer-Reviewed Original ResearchConceptsExtended X-ray absorption fine structureFemtosecond x-ray diffractionX-ray diffractionOxygen-evolving complexS3 stateHybrid quantum mechanics/molecular mechanics (QM/MM) methodX-ray absorption fine structureQuantum mechanics/molecular mechanics methodsAbsorption fine structureQM/MMPhotosystem IIMolecular mechanics methodElectron paramagnetic resonanceWater ligandsS3 transitionAmmonia bindingParamagnetic resonanceFine structureMechanics methodDiffractionComplexesStateResonanceLigandsMn4
2015
Crystallographic study of a MATE transporter presents a difficult case in structure determination with low‐resolution, anisotropic data and crystal twinning
Symersky J, Guo Y, Wang J, Lu M. Crystallographic study of a MATE transporter presents a difficult case in structure determination with low‐resolution, anisotropic data and crystal twinning. Acta Crystallographica Section D, Structural Biology 2015, 71: 2287-2296. PMID: 26527145, PMCID: PMC4631480, DOI: 10.1107/s1399004715016995.Peer-Reviewed Original ResearchEstimation of the quality of refined protein crystal structures
Wang J. Estimation of the quality of refined protein crystal structures. Protein Science 2015, 24: 661-669. PMID: 25581292, PMCID: PMC4420517, DOI: 10.1002/pro.2639.Peer-Reviewed Original ResearchAnalysis of the Radiation-Damage-Free X‑ray Structure of Photosystem II in Light of EXAFS and QM/MM Data
Askerka M, Vinyard DJ, Wang J, Brudvig GW, Batista VS. Analysis of the Radiation-Damage-Free X‑ray Structure of Photosystem II in Light of EXAFS and QM/MM Data. Biochemistry 2015, 54: 1713-1716. PMID: 25710258, DOI: 10.1021/acs.biochem.5b00089.Peer-Reviewed Original ResearchConceptsPhotosystem II crystalsX-ray absorption fine structureExtended X-ray absorption fine structureAbsorption fine structurePhotosystem IIHigh-resolution structural modelS1 stateS0 stateOxygen-evolving complexRadiation damageX-ray diffraction studiesExtensive dark adaptationFine structureDiffraction studiesOxygen atomsManganese centersX-ray structureAtomsMM dataCrystalsStateEXAFSLightStructureResolution
2014
On the validation of crystallographic symmetry and the quality of structures
Wang J. On the validation of crystallographic symmetry and the quality of structures. Protein Science 2014, 24: 621-632. PMID: 25352397, PMCID: PMC4420513, DOI: 10.1002/pro.2595.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayDatabases, ProteinModels, MolecularProtein ConformationProteinsSoftwareX-Ray DiffractionExploiting subtle structural differences in heavy‐atom derivatives for experimental phasing
Wang J, Li Y, Modis Y. Exploiting subtle structural differences in heavy‐atom derivatives for experimental phasing. Acta Crystallographica Section D, Structural Biology 2014, 70: 1873-1883. PMID: 25004964, PMCID: PMC4089484, DOI: 10.1107/s1399004714008943.Peer-Reviewed Original ResearchProtein ConformationViral Envelope ProteinsStructural models of the membrane anchors of envelope glycoproteins E1 and E2 from pestiviruses
Wang J, Li Y, Modis Y. Structural models of the membrane anchors of envelope glycoproteins E1 and E2 from pestiviruses. Virology 2014, 454: 93-101. PMID: 24725935, PMCID: PMC3986810, DOI: 10.1016/j.virol.2014.02.015.Peer-Reviewed Original ResearchMeSH KeywordsGlycoproteinsModels, MolecularPestivirusProtein ConformationProtein MultimerizationViral Envelope ProteinsExploiting large non‐isomorphous differences for phase determination of a G‐segment invertase–DNA complex
Ritacco CJ, Steitz TA, Wang J. Exploiting large non‐isomorphous differences for phase determination of a G‐segment invertase–DNA complex. Acta Crystallographica Section D, Structural Biology 2014, 70: 685-693. PMID: 24598738, PMCID: PMC3949525, DOI: 10.1107/s1399004713032392.Peer-Reviewed Original Research
2013
Crystal structure of glycoprotein E2 from bovine viral diarrhea virus
Li Y, Wang J, Kanai R, Modis Y. Crystal structure of glycoprotein E2 from bovine viral diarrhea virus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 6805-6810. PMID: 23569276, PMCID: PMC3637714, DOI: 10.1073/pnas.1300524110.Peer-Reviewed Original ResearchConceptsBovine viral diarrhea virus (BVDV) E2C-terminal motifHost cell cytoplasmImportant animal pathogenMembrane fusion mechanismIg-like domainsUnique protein architectureOuter lipid envelopeProtein architectureAnimal pathogensFusion apparatusStructure of E2New foldCellular membranesBovine viral diarrhea virusAromatic residuesViral diarrhea virusCell cytoplasmLipid envelopeDisulfide bondsCell entryDiarrhea virusMajor global health threatCrystal structureFusion mechanism
2012
Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase
Ritacco CJ, Kamtekar S, Wang J, Steitz TA. Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase. Nucleic Acids Research 2012, 41: 2673-2682. PMID: 23275567, PMCID: PMC3575834, DOI: 10.1093/nar/gks1303.Peer-Reviewed Original ResearchContribution of Partial Charge Interactions and Base Stacking to the Efficiency of Primer Extension at and beyond Abasic Sites in DNA
Xia S, Vashishtha A, Bulkley D, Eom SH, Wang J, Konigsberg WH. Contribution of Partial Charge Interactions and Base Stacking to the Efficiency of Primer Extension at and beyond Abasic Sites in DNA. Biochemistry 2012, 51: 4922-4931. PMID: 22630605, PMCID: PMC3426629, DOI: 10.1021/bi300296q.Peer-Reviewed Original ResearchUsing a Fluorescent Cytosine Analogue tCo To Probe the Effect of the Y567 to Ala Substitution on the Preinsertion Steps of dNMP Incorporation by RB69 DNA Polymerase
Xia S, Beckman J, Wang J, Konigsberg WH. Using a Fluorescent Cytosine Analogue tCo To Probe the Effect of the Y567 to Ala Substitution on the Preinsertion Steps of dNMP Incorporation by RB69 DNA Polymerase. Biochemistry 2012, 51: 4609-4617. PMID: 22616982, PMCID: PMC3437246, DOI: 10.1021/bi300241m.Peer-Reviewed Original ResearchProbing Minor Groove Hydrogen Bonding Interactions between RB69 DNA Polymerase and DNA
Xia S, Christian TD, Wang J, Konigsberg WH. Probing Minor Groove Hydrogen Bonding Interactions between RB69 DNA Polymerase and DNA. Biochemistry 2012, 51: 4343-4353. PMID: 22571765, PMCID: PMC3374494, DOI: 10.1021/bi300416z.Peer-Reviewed Original ResearchBidentate and tridentate metal‐ion coordination states within ternary complexes of RB69 DNA polymerase
Xia S, Eom SH, Konigsberg WH, Wang J. Bidentate and tridentate metal‐ion coordination states within ternary complexes of RB69 DNA polymerase. Protein Science 2012, 21: 447-451. PMID: 22238207, PMCID: PMC3375444, DOI: 10.1002/pro.2026.Peer-Reviewed Original ResearchConceptsCoordination complexesMetal ionsCoordination stateSecond metal ionMetal ion coordinationDivalent metal ionsTernary complexTridentate coordinationBond formationPhosphorus atomActive siteRelevant conformationsStructural studiesSelectivity mechanismIonsTriphosphate tailComplexesRB69 DNA polymeraseÅ resolutionBase selectivityGround stateSubstrate alignmentPolymerase active siteCatalysisCoordination