2023
Separating Inner and Outer Membranes of Escherichia coli by EDTA-free Sucrose Gradient Centrifugation
Shu S, Mi W. Separating Inner and Outer Membranes of Escherichia coli by EDTA-free Sucrose Gradient Centrifugation. Bio-protocol 2023, 13: e4638. PMID: 36968434, PMCID: PMC10031520, DOI: 10.21769/bioprotoc.4638.Peer-Reviewed Original ResearchInner membraneOuter membraneGram-negative bacteriaPeptidoglycan cell wallEscherichia coliMembrane protein purificationTotal cell membranesSucrose gradient centrifugationMembrane proteinsCell wallProtein structureFunctional studiesProtein purificationTotal membranesCell membraneSucrose gradientsBiochemical proceduresGradient centrifugationProteinMembraneColiBacteriaGradient ultracentrifugationLipidsUltracentrifugation method
2022
Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli
Shu S, Mi W. Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli. Nature Communications 2022, 13: 4576. PMID: 35931690, PMCID: PMC9356133, DOI: 10.1038/s41467-022-32277-1.Peer-Reviewed Original ResearchConceptsRegulatory mechanismsAnti-adaptor proteinsFirst committed stepMost Gram-negative bacteriaEssential glycolipidEssential membraneGram-negative bacteriaTransmembrane helicesAdaptor proteinCommitted stepCytoplasmic domainFtsHLPS synthesisAnalysis unravelsLipopolysaccharide synthesisLapBEscherichia coliE. coliPermeability barrierProtein levelsLpxCProtease activityProteinColiYejM
2017
Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3
Schoebel S, Mi W, Stein A, Ovchinnikov S, Pavlovicz R, DiMaio F, Baker D, Chambers MG, Su H, Li D, Rapoport TA, Liao M. Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3. Nature 2017, 548: 352-355. PMID: 28682307, PMCID: PMC5736104, DOI: 10.1038/nature23314.Peer-Reviewed Original Research
2015
Single-particle electron microscopy in the study of membrane protein structure
De Zorzi R, Mi W, Liao M, Walz T. Single-particle electron microscopy in the study of membrane protein structure. Microscopy 2015, 65: 81-96. PMID: 26470917, PMCID: PMC4749050, DOI: 10.1093/jmicro/dfv058.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsSingle-particle electron microscopyMembrane protein structuresMembrane proteinsProtein structureAtomic modelElectron microscopyMore membrane proteinsUnprecedented qualityTransient receptor potential (TRP) channel familyDevice cameraChannel familyProteinStructure refinementMicroscopyStructureEnhanced potentialMinor roleCrystalsTechnical advancesTechnical limitationsGreat advantageShort orderFamily