2017
On contribution of known atomic partial charges of protein backbone in electrostatic potential density maps
Wang J. On contribution of known atomic partial charges of protein backbone in electrostatic potential density maps. Protein Science 2017, 26: 1098-1104. PMID: 28370507, PMCID: PMC5441424, DOI: 10.1002/pro.3169.Peer-Reviewed Original ResearchConceptsAtomic partial chargesPartial chargesQuantum mechanicsForce field parametersAtomic propertiesPartial atomic chargesDensity mapsAtomic chargesField parametersMolecular dynamicsAtomsElectron microscopyProtein backboneNeutral peptide backboneChargeChain atomsComputer simulationsSide-chain atomsDensityPeptide backboneProtein moleculesModel refinementSimulationsPotential densityBackboneSystematic analysis of residual density suggests that a major limitation in well‐refined X‐ray structures of proteins is the omission of ordered solvent
Wang J. Systematic analysis of residual density suggests that a major limitation in well‐refined X‐ray structures of proteins is the omission of ordered solvent. Protein Science 2017, 26: 1012-1023. PMID: 28244185, PMCID: PMC5405434, DOI: 10.1002/pro.3145.Peer-Reviewed Original Research
2016
Oxygen additions in serial femtosecond crystallographic protein structures
Wang J. Oxygen additions in serial femtosecond crystallographic protein structures. Protein Science 2016, 25: 1797-1802. PMID: 27438534, PMCID: PMC5029527, DOI: 10.1002/pro.2987.Peer-Reviewed Original Research
2015
Estimation 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 Research
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 Research
2004
Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily
Wang J. Nucleotide-dependent domain motions within rings of the RecA/AAA+ superfamily. Journal Of Structural Biology 2004, 148: 259-267. PMID: 15522774, DOI: 10.1016/j.jsb.2004.07.003.Peer-Reviewed Original ResearchConceptsNucleotide-dependent conformational changesT7 DNA helicaseImportant biological functionsMechanochemical motorOligomeric ringsDNA helicaseBiological functionsF1-ATPaseConformational changesDomain motionProteinMechanistic workForce generationHslUHelicaseFoldsChemical energyATPFamilyRing structureDomainMembers
1997
The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
Wang J, Hartling J, Flanagan J. The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis. Cell 1997, 91: 447-456. PMID: 9390554, DOI: 10.1016/s0092-8674(00)80431-6.Peer-Reviewed Original Research