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- EMDB-24489: The C1b projection within the ciliary central apparatus from the ... -

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Basic information

Entry
Database: EMDB / ID: EMD-24489
TitleThe C1b projection within the ciliary central apparatus from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas fap413 mutant axonemes
Map datafap413 mutant C1b projection
Sample
  • Organelle or cellular component: The C1b projection within the the ciliary central apparatus from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas wild type axonemes
Biological speciesChlamydomonas reinhardtii (plant)
Methodelectron tomography / cryo EM / Resolution: 25.0 Å
AuthorsCai K / Nicastro D
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM083122 United States
Cancer Prevention and Research Institute of Texas (CPRIT)RR140082 United States
CitationJournal: J Cell Sci / Year: 2021
Title: Structural organization of the C1b projection within the ciliary central apparatus.
Authors: Kai Cai / Yanhe Zhao / Lei Zhao / Nhan Phan / Yuqing Hou / Xi Cheng / George B Witman / Daniela Nicastro /
Abstract: Motile cilia have a '9+2' structure containing nine doublet microtubules and a central apparatus (CA) composed of two singlet microtubules with associated projections. The CA plays crucial roles in ...Motile cilia have a '9+2' structure containing nine doublet microtubules and a central apparatus (CA) composed of two singlet microtubules with associated projections. The CA plays crucial roles in regulating ciliary motility. Defects in CA assembly or function usually result in motility-impaired or paralyzed cilia, which in humans causes disease. Despite their importance, the protein composition and functions of most CA projections remain largely unknown. Here, we combined genetic, proteomic and cryo-electron tomographic approaches to compare the CA of wild-type Chlamydomonas reinhardtii with those of three CA mutants. Our results show that two proteins, FAP42 and FAP246, are localized to the L-shaped C1b projection of the CA, where they interact with the candidate CA protein FAP413. FAP42 is a large protein that forms the peripheral 'beam' of the C1b projection, and the FAP246-FAP413 subcomplex serves as the 'bracket' between the beam (FAP42) and the C1b 'pillar' that attaches the projection to the C1 microtubule. The FAP246-FAP413-FAP42 complex is essential for stable assembly of the C1b, C1f and C2b projections, and loss of these proteins leads to ciliary motility defects.
History
DepositionJul 21, 2021-
Header (metadata) releaseNov 3, 2021-
Map releaseNov 3, 2021-
UpdateNov 24, 2021-
Current statusNov 24, 2021Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 123
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by height
  • Surface level: 123
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_24489.png

Downloads & links

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Map

FileDownload / File: emd_24489.map.gz / Format: CCP4 / Size: 2.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationfap413 mutant C1b projection
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
3.15 Å/pix.
x 92 pix.
= 289.892 Å		3.15 Å/pix.
x 86 pix.
= 270.986 Å		3.15 Å/pix.
x 88 pix.
= 277.288 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 3.151 Å
Density

Histogram

Histogram (log scale)
Contour LevelMovie #1: 123
Minimum - Maximum115.6481 - 135.80162
Average (Standard dev.)126.8058 (±2.0756114)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-93-101-179
Dimensions868892
Spacing888692
CellA: 277.288 Å / B: 270.986 Å / C: 289.892 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z3.1513.1513.151
M x/y/z888692
origin x/y/z0.0000.0000.000
length x/y/z277.288270.986289.892
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ320320320
MAP C/R/S123
start NC/NR/NS-101-93-179
NC/NR/NS888692
D min/max/mean115.648135.802126.806

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Supplemental data

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Sample components

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Entire : The C1b projection within the the ciliary central apparatus from ...

EntireName: The C1b projection within the the ciliary central apparatus from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas wild type axonemes
Components
  • Organelle or cellular component: The C1b projection within the the ciliary central apparatus from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas wild type axonemes

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Supramolecule #1: The C1b projection within the the ciliary central apparatus from ...

SupramoleculeName: The C1b projection within the the ciliary central apparatus from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas wild type axonemes
type: organelle_or_cellular_component / ID: 1 / Parent: 0
Source (natural)Organism: Chlamydomonas reinhardtii (plant)

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Experimental details

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Structure determination

Methodcryo EM
Processingelectron tomography
Aggregation statecell

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Sample preparation

BufferpH: 7.4
GridModel: Quantifoil R2/2 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Instrument: HOMEMADE PLUNGER
SectioningOther: NO SECTIONING
Fiducial markerManufacturer: Sigma Aldrich / Diameter: 10 nm

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsPhase plate: VOLTA PHASE PLATE
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Detector mode: COUNTING / Average electron dose: 1.5 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionAlgorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 25.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: eTomo / Number images used: 1401

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