Huaxin Yu
Postdoctoral AssociateDownloadHi-Res Photo
About
Copy Link
Titles
Postdoctoral Associate
Appointments
Microbial Pathogenesis
Postdoctoral AssociatePrimary
Other Departments & Organizations
Education & Training
- PhD
- University of Hyogo, Picobiology (2022)
- PA
- Okayama University, Research Institute for Interdisciplinary Science (2022)
- BS
- Jilin University, Life Science
Research
Copy Link
Overview
Medical Research Interests
Cryoelectron Microscopy; Electronic Data Processing; Informatics; Microbiology; Molecular Structure; Programming Languages; Tomography
ORCID
0000-0002-9375-1916- View Lab Website
Liu Lab
Research at a Glance
Yale Co-Authors
Frequent collaborators of Huaxin Yu's published research.
Publications Timeline
A big-picture view of Huaxin Yu's research output by year.
Research Interests
Research topics Huaxin Yu is interested in exploring.
Jun Liu, PhD
Chunyan Wang, PhD
Wangbiao (Seven) Guo
7Publications
151Citations
Cryoelectron Microscopy
Publications
2026
Assembly and glycosylation of Helicobacter pylori sheathed flagella
Kumar R, Tachiyama S, Yu H, Heydari S, Guo J, Botting J, Guo W, Hoover T, Liu J. Assembly and glycosylation of Helicobacter pylori sheathed flagella. PNAS Nexus 2026, 5: pgag011. PMID: 41659214, PMCID: PMC12880188, DOI: 10.1093/pnasnexus/pgag011.Peer-Reviewed Original ResearchAltmetricConceptsSheathed flagellaSingle-particle cryo-electron microscopySurface-exposed domainsMembranous sheathIntra-subunit contactsCryo-electron microscopyNear-atomic structureFlagellin FlaAColonization nicheComplex nanomachinesDiverse speciesBacterial flagellaFlagellar filamentsGastric nicheFlagellaAcidic glycansMolecular basisUnique adaptationsFlaAFlagellinFlaBMotilityFilamentsNicheMolecular frameworkStructural Basis for Bacteriophage P22 Assembly and Infection Initiation
Wang C, Yu H, Park T, Molineux I, Liu J. Structural Basis for Bacteriophage P22 Assembly and Infection Initiation. Journal Of Molecular Biology 2026, 438: 169647. PMID: 41565001, PMCID: PMC12854149, DOI: 10.1016/j.jmb.2026.169647.Peer-Reviewed Original ResearchAltmetricMeSH Keywords and ConceptsConceptsCryo-EM structureE proteinSalmonella phage P22Wild-type P22Cryo-electron tomographyPhage P22Tail apparatusCapsid interiorLoop residuesStructural basisInfection initiationCell surfaceCapsidInternalized EP22Gp10Symmetry mismatchExtracellular channelsGP1AssemblyTailspikeMutantsBacteriophageAdaptorSalmonella
2025
Structural basis of bacteriophage Ur-lambda infection initiation
Yu H, Wang C, Yue J, Guo W, Molineux I, Liu J. Structural basis of bacteriophage Ur-lambda infection initiation. Science Advances 2025, 11: eadw7914. PMID: 41237242, PMCID: PMC12617516, DOI: 10.1126/sciadv.adw7914.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and Concepts
2024
Broadly conserved FlgV controls flagellar assembly and Borrelia burgdorferi dissemination in mice
Zamba-Campero M, Soliman D, Yu H, Lasseter A, Chang Y, Silberman J, Liu J, Aravind L, Jewett M, Storz G, Adams P. Broadly conserved FlgV controls flagellar assembly and Borrelia burgdorferi dissemination in mice. Nature Communications 2024, 15: 10417. PMID: 39614093, PMCID: PMC11607428, DOI: 10.1038/s41467-024-54806-w.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsFlagellar assemblyFlagellar componentsComplex hierarchical regulatory networkRNA-binding protein HfqFlagellar basal bodyHierarchical regulatory networkB. burgdorferiProtein HfqRegulatory networksBasal bodiesFlagellar filamentsCell divisionMotile bacteriaSpirochete motilitySpirochete Borrelia burgdorferiEnzootic cycleGenesMotilityS28AssemblySuperoperonHfqSpirochetesEpsilonproteobacteriaFlagellaOxygen-evolving photosystem II structures during S1–S2–S3 transitions
Li H, Nakajima Y, Nango E, Owada S, Yamada D, Hashimoto K, Luo F, Tanaka R, Akita F, Kato K, Kang J, Saitoh Y, Kishi S, Yu H, Matsubara N, Fujii H, Sugahara M, Suzuki M, Masuda T, Kimura T, Thao T, Yonekura S, Yu L, Tosha T, Tono K, Joti Y, Hatsui T, Yabashi M, Kubo M, Iwata S, Isobe H, Yamaguchi K, Suga M, Shen J. Oxygen-evolving photosystem II structures during S1–S2–S3 transitions. Nature 2024, 626: 670-677. PMID: 38297122, PMCID: PMC10866707, DOI: 10.1038/s41586-023-06987-5.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsS-state transitionsWater moleculesPhotosystem II structureO-O bond formationFast transfer of electronsD1 subunitSub-microsecond timescaleStructural dynamicsFast transferOxidation of waterSequence of electron transferAmino acid residuesSerial femtosecond crystallographyS3 stateTransfer of electronsSi statesMn4CaO5 clusterD1 subunit of PSIIFour-step cycleElectron transferNanosecond timescaleMetal clustersBond formationAcid residuesFemtosecond crystallography
2022
Excited-state intermediates in a designer protein encoding a phototrigger caught by an X-ray free-electron laser
Liu X, Liu P, Li H, Xu Z, Jia L, Xia Y, Yu M, Tang W, Zhu X, Chen C, Zhang Y, Nango E, Tanaka R, Luo F, Kato K, Nakajima Y, Kishi S, Yu H, Matsubara N, Owada S, Tono K, Iwata S, Yu L, Shen J, Wang J. Excited-state intermediates in a designer protein encoding a phototrigger caught by an X-ray free-electron laser. Nature Chemistry 2022, 14: 1054-1060. PMID: 35851837, DOI: 10.1038/s41557-022-00992-3.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsExcited-state intermediatesX-ray free-electron lasersTR-SFXReaction intermediatesC-H bond activationC-H bond transformationsTime-resolved serial femtosecond crystallographyX-rayFree-electron laserSerial femtosecond crystallographyBond activationC-HBond transformationsFemtosecond crystallographyPhotoactive proteinsChemistry researchQuantum efficiencyAtomic motionPhototriggerIntermediateRedox enzymesReactionFlash illuminationCrystallographyDesigning proteins
2021
Cryo-EM structure of monomeric photosystem II at 2.78 Å resolution reveals factors important for the formation of dimer
Yu H, Hamaguchi T, Nakajima Y, Kato K, Kawakami K, Akita F, Yonekura K, Shen J. Cryo-EM structure of monomeric photosystem II at 2.78 Å resolution reveals factors important for the formation of dimer. Biochimica Et Biophysica Acta (BBA) - Bioenergetics 2021, 1862: 148471. PMID: 34216574, DOI: 10.1016/j.bbabio.2021.148471.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMonomeric PSIICryo-EM structureMonomer-monomer interfaceSulfoquinovosyl diacylglycerolPhotosystem IICryo-EMPhotosystem II monomerPhotosystem II dimersA-resolutionLow-resolution crystal structureCryo-EM density mapsCrystal structurePsbO subunitCryo-electron microscopyPSII monomersSynechocystis sp.Function in vivoMonomer structureExtrinsic proteinsWater oxidation reactionAnalogous regionLight energy conversionPsbOFormation of dimersDensity maps
Get In Touch
Copy Link
Contacts
Email