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- PDB-6fu8: uL23 beta hairpin loop deletion of E.coli ribosome -

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Basic information

Entry
Database: PDB / ID: 6fu8
TitleuL23 beta hairpin loop deletion of E.coli ribosome
Components50S ribosomal protein L23
KeywordsRIBOSOMAL PROTEIN / uL23 / loop deletion / ribosomal tunnel
Function / homologyRibosomal protein L23/L25, conserved site / Nucleotide-binding alpha-beta plait domain superfamily / Ribosomal protein L23/L15e core domain superfamily / Ribosomal protein L25/L23 / Ribosomal protein L23 / Ribosomal protein L23 signature. / ribosome / rRNA binding / structural constituent of ribosome / translation / 50S ribosomal protein L23
Function and homology information
Specimen sourceEscherichia coli O157:H7 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 3.2 Å resolution
AuthorsKudva, R. / von Heijne, G. / Carroni, M.
Funding supportSweden , 1 items
OrganizationGrant numberCountry
Knut and Alice Wallenberg FoundationSweden
CitationJournal: Elife / Year: 2018
Title: The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding.
Authors: Renuka Kudva / Pengfei Tian / Fátima Pardo-Avila / Marta Carroni / Robert B Best / Harris D Bernstein / Gunnar von Heijne
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Feb 26, 2018 / Release: Dec 5, 2018
RevisionDateData content typeGroupCategoryItemProviderType
1.0Dec 5, 2018Structure modelrepositoryInitial release
1.1Dec 26, 2018Structure modelData collection / Database referencescitation / citation_author_citation.title / _citation_author.identifier_ORCID / _citation_author.name

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Assembly

Deposited unit
C: 50S ribosomal protein L23


Theoretical massNumber of molelcules
Total (without water)9,3241
Polyers9,3241
Non-polymers00
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551
Buried area (Å2)0
ΔGint (kcal/M)0
Surface area (Å2)5880
MethodPISA

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Components

#1: Protein/peptide 50S ribosomal protein L23 /


Mass: 9324.003 Da / Num. of mol.: 1 / Source: (gene. exp.) Escherichia coli O157:H7 (bacteria) / Gene: rplW, Z4689, ECs4183 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ADZ2

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / Reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: E.coli ribosome with beta-hairpin of uL23 deleted / Type: RIBOSOME
Details: Deposited PDB is of the uL23 with the beta-hairpin loop deleted.
Entity ID: 1 / Source: RECOMBINANT
Molecular weightValue: 2.6 MDa / Experimental value: NO
Source (natural)Organism: Escherichia coli (E. coli)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 400
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 kelvins

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 microns / Alignment procedure: ZEMLIN TABLEAU
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 1.17 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k) / Number of grids imaged: 1 / Number of real images: 3500
Image scansMovie frames/image: 20

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Processing

EM software
IDNameVersionCategory
2EPU1.09image acquisition
4CTFFIND4CTF correction
7UCSF Chimeramodel fitting
12cryoSPARC3D reconstruction
13Cootmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNumber of particles selected: 471272
SymmetryPoint symmetry: C1
3D reconstructionResolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 132029 / Algorithm: BACK PROJECTION
Details: All processing from ab initio to refinement and sharpening performed in cryosparc
Number of class averages: 1 / Symmetry type: POINT
Atomic model buildingRef protocol: RIGID BODY FIT

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