2022
How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM
Wang J, Liu J, Gisriel CJ, Wu S, Maschietto F, Flesher DA, Lolis E, Lisi GP, Brudvig GW, Xiong Y, Batista VS. How to correct relative voxel scale factors for calculations of vector-difference Fourier maps in cryo-EM. Journal Of Structural Biology 2022, 214: 107902. PMID: 36202310, PMCID: PMC10226527, DOI: 10.1016/j.jsb.2022.107902.Peer-Reviewed Original ResearchConceptsCryo-EM mapsAmino acid residuesAcid residuesCryo-electron microscopy mapIndividual amino acid residuesCyanobacteria Synechocystis spPCC 6803Synechocystis spMicroscopy mapsThermosynechococcus elongatusSARS-CoV-2 spike proteinLocal structural changesResiduesSpike proteinAtomic coordinatesElongatusSubunitsSpeciesProteinSpSimilar structureStructural changes
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 ResearchConceptsCryo-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
2020
Cryo-EM Structure of Monomeric Photosystem II from Synechocystis sp. PCC 6803 Lacking the Water-Oxidation Complex
Gisriel C, Zhou K, Huang H, Debus R, Xiong Y, Brudvig G. Cryo-EM Structure of Monomeric Photosystem II from Synechocystis sp. PCC 6803 Lacking the Water-Oxidation Complex. Joule 2020, 4: 2131-2148. DOI: 10.1016/j.joule.2020.07.016.Peer-Reviewed Original ResearchOxygen-evolving complexPhotosystem II enzymeWater oxidation complexWater oxidationMetal clustersMechanism of photoactivationActive siteMonomeric photosystem IIPhotosystem IICryo-EM structureStructural rearrangementsComplexesPhotoactivationSynechocystis spPeripheral subunitsCationsComputational techniquesOxidationOverall biogenesisStructureMesophilic cyanobacteriumOxygenPCC 6803II enzymesPSII
2005
Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*
Bautista J, Tracewell C, Schlodder E, Cunningham F, Brudvig G, Diner B. Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*. Journal Of Biological Chemistry 2005, 280: 38839-38850. PMID: 16159754, DOI: 10.1074/jbc.m504953200.Peer-Reviewed Original ResearchMeSH Keywordsbeta CaroteneCarotenoidsCationsChlorophyllChromatographyChromatography, High Pressure LiquidElectronsGene DeletionLightManganeseModels, ChemicalModels, MolecularMutationOxidation-ReductionOxidoreductasesOxygenPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPigmentationRhodobacter capsulatusSpectrophotometrySpectrophotometry, InfraredSynechocystisTemperatureTime FactorsTyrosineConceptsPhytoene desaturase geneII core complexesDesaturase genePS II core complexesSynechocystis spCore complexPS II assemblyCarotene desaturase genePhotosystem II core complexPCC 6803Rhodobacter capsulatusWild typeMutant strainRedox functionPhotosystem IISecondary electron transfer pathwayGenesElectron transfer pathwayLight-induced formationCarotenoidsSpChlorophyllConjugated pi-electron systemPathwayComplexes
1992
Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression.
Verkamp E, Jahn M, Jahn D, Kumar A, Söll D. Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. Journal Of Biological Chemistry 1992, 267: 8275-8280. PMID: 1569081, DOI: 10.1016/s0021-9258(18)42438-6.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAmino Acid SequenceBase SequenceChromatography, GelCyanobacteriaEscherichia coliGene ExpressionGenes, BacterialGenes, FungalGenetic Complementation TestMolecular Sequence DataOpen Reading FramesPlasmidsRestriction MappingSaccharomyces cerevisiaeSequence Homology, Nucleic AcidConceptsGlutamyl-tRNA reductaseHemA geneAmino acid sequenceHemA proteinGluTR activitySynechocystis 6803Acid sequenceE. coliGlutamate-1-semialdehyde aminotransferaseHemA gene productEscherichia coliCyanobacterium Synechocystis spOpen reading frameEnterobacterium Escherichia coliDNA sequence analysisFunctional complementationGene structureGlu-tRNAGel filtration experimentsPCC 6803Synechocystis spGlutamyl-tRNAAcid polypeptideReading frameALA formation
1990
Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis
O'Neill G, Söll D. Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis. Journal Of Bacteriology 1990, 172: 6363-6371. PMID: 2121711, PMCID: PMC526821, DOI: 10.1128/jb.172.11.6363-6371.1990.Peer-Reviewed Original ResearchConceptsSynechocystis 6803Synechocystis spFirst anticodon baseStrain PCC 6803Cyanobacterium Synechocystis spTotal tRNA populationAmount of chlorophyllNorthern blot analysisChlorophyll biosynthesisALA biosynthesisPrecursor tRNAsPCC 6803TRNA speciesProtein biosynthesisTRNA populationCellular RNAAminoacylation assaysChlorophyll levelsBiosynthesisAddition of inhibitorsBlot analysisTranslation systemDelta-aminolevulinic acidTRNAChlorophyll
1988
Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species
O'Neill G, Peterson D, Schön A, Chen M, Söll D. Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species. Journal Of Bacteriology 1988, 170: 3810-3816. PMID: 2900830, PMCID: PMC211375, DOI: 10.1128/jb.170.9.3810-3816.1988.Peer-Reviewed Original ResearchConceptsPrecursor delta-aminolevulinic acidHigher plantsUnicellular cyanobacterium Synechocystis spGlutamate-1-semialdehyde aminotransferaseCell extractsCyanobacterium Synechocystis spDelta-aminolevulinic acidSouthern blot analysisIdentical primary sequencesSynechocystis spNucleotide modificationsConversion of glutamateGene copiesALA synthesisPrimary sequenceSequence specificityTerminal enzymePolyacrylamide gel electrophoresisChloroplastsEuglena gracilisEscherichia coliSpeciesBlot analysisTRNAGel electrophoresis
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