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- PDB-6oua: Cryo-EM structure of the yeast Ctf3 complex -

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Entry
Database: PDB / ID: 6oua
TitleCryo-EM structure of the yeast Ctf3 complex
Components
  • Inner kinetochore subunit CTF3
  • Inner kinetochore subunit MCM16
  • Inner kinetochore subunit MCM22
KeywordsCELL CYCLE / kinetochore / chromosome / cryo-em
Function / homology
Function and homology information


establishment of mitotic sister chromatid cohesion / condensed nuclear chromosome kinetochore / DNA replication initiation / mitotic spindle assembly checkpoint / chromosome segregation / meiotic cell cycle / cell division
Inner kinetochore subunit MCM22 / Inner kinetochore subunit MCM16 / Inner kinetochore subunit CTF3
Specimen sourceSaccharomyces cerevisiae (baker's yeast)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.18 Å
AuthorsHinshaw, S.M. / Harrison, S.C.
Funding supportUnited States , 1件
OrganizationGrant numberCountry
Howard Hughes Medical InstituteUnited States
CitationJournal: To Be Published
Title: The structure of the yeast Ctf3 complex
Authors: Hinshaw, S.M. / Dates, D.N. / Harrison, S.C.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: May 4, 2019 / Release: May 15, 2019Array

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Structure visualization

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Assembly

Deposited unit
I: Inner kinetochore subunit CTF3
H: Inner kinetochore subunit MCM16
K: Inner kinetochore subunit MCM22


Theoretical massNumber of molelcules
Total (without water)133,9313
Polymers133,9313
Non-polymers00
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein/peptide Inner kinetochore subunit CTF3 / CENP-I homolog / Chromosome loss protein 3 / Chromosome transmission fidelity protein 3 / Constitutive centromere-associated network protein CTF3


Mass: 84617.891 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Production host: Escherichia coli (E. coli) / References: UniProt: Q12748
#2: Protein/peptide Inner kinetochore subunit MCM16 / CENP-H homolog / Constitutive centromere-associated network protein MCM16 / Minichromosome maintenance protein 16


Mass: 21438.359 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Production host: Escherichia coli (E. coli) / References: UniProt: Q12262
#3: Protein/peptide Inner kinetochore subunit MCM22 / CENP-K homolog / Constitutive centromere-associated network protein MCM22 / Minichromosome maintenance protein 22


Mass: 27874.799 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Production host: Escherichia coli (E. coli) / References: UniProt: P47167

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Ctf3 complex / Type: COMPLEX / Entity ID: 1, 2, 3 / Source: RECOMBINANT
Source (natural)Organism: Saccharomyces cerevisiae (baker's yeast)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8.5
SpecimenDetails: Recombinant protein frozen in vitreous ice / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid type: C-flat-2/2
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 105000 X / Cs: 2.7 mm / C2 aperture diameter: 50 µns
Specimen holderCryogen: NITROGEN / Model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 50.7 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1

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Processing

SoftwareName: PHENIX / Version: 1.13_2998: / Classification: refinement
EM softwareName: SerialEM / Version: 3.7 / Category: image acquisition
Image processingDetails: Counting mode
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 4.18 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 71632 / Symmetry type: POINT
Atomic model buildingSpace: REAL

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