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
Analysis 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 DiffractionDiamonds in the rough: a strong case for the inclusion of weak‐intensity X‐ray diffraction data
Wang J, Wing RA. Diamonds in the rough: a strong case for the inclusion of weak‐intensity X‐ray diffraction data. Acta Crystallographica Section D, Structural Biology 2014, 70: 1491-1497. PMID: 24816117, PMCID: PMC4014128, DOI: 10.1107/s1399004714005318.Peer-Reviewed Original ResearchExploiting 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
2012
Structural Basis for Differential Insertion Kinetics of dNMPs Opposite a Difluorotoluene Nucleotide Residue
Xia S, Eom SH, Konigsberg WH, Wang J. Structural Basis for Differential Insertion Kinetics of dNMPs Opposite a Difluorotoluene Nucleotide Residue. Biochemistry 2012, 51: 1476-1485. PMID: 22304682, PMCID: PMC3292180, DOI: 10.1021/bi2016487.Peer-Reviewed Original Research
2005
A Twisted Four-Sheeted Model for an Amyloid Fibril
Wang J, Gülich S, Bradford C, Ramirez-Alvarado M, Regan L. A Twisted Four-Sheeted Model for an Amyloid Fibril. Structure 2005, 13: 1279-1288. PMID: 16154085, DOI: 10.1016/j.str.2005.06.010.Peer-Reviewed Original ResearchMeSH KeywordsAmyloidBacterial ProteinsHumansModels, MolecularProtein Structure, SecondaryX-Ray Diffraction
2004
Correction of X‐ray intensities from single crystals containing lattice‐translocation defects
Wang J, Kamtekar S, Berman AJ, Steitz TA. Correction of X‐ray intensities from single crystals containing lattice‐translocation defects. Acta Crystallographica Section D, Structural Biology 2004, 61: 67-74. PMID: 15608377, DOI: 10.1107/s0907444904026721.Peer-Reviewed Original Research
2000
Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond
Li F, Wang J, Steitz T. Sulfolobus shibatae CCA-adding enzyme forms a tetramer upon binding two tRNA molecules: a scrunching-shuttling model of CCA specificity1 1Edited by T. Richmond. Journal Of Molecular Biology 2000, 304: 483-492. PMID: 11090289, DOI: 10.1006/jmbi.2000.4189.Peer-Reviewed Original ResearchConceptsActive siteMulti-angle laser lightSmall-angle X-ray scatteringSize exclusion chromatographyX-ray scatteringFurther dimerizationExclusion chromatographyMoleculesDimeric enzymeC basesOligomerization stateTetramerTransfer RNA moleculesLaser lightTRNA moleculesRNA moleculesMonomersPrimer strandChromatographyEnzymeDimersHigh specificityBindingCCA-adding enzymeDimerization