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- EMDB-8817: TFIIH reconstruction from particles sorted for the XPD FeS-cluste... -

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Entry
Database: EMDB / ID: 8817
TitleTFIIH reconstruction from particles sorted for the XPD FeS-cluster domain using signal-subtracted classification.
Map dataTFIIH reconstruction from particles sorted for the FeS-cluster domain using signal-subtracted classification.
SampleTranscription factor IIH (TFIIH):
Function / homologyTFIIH C1-like domain / Helicase conserved C-terminal domain / Helicase-like, DEXD box c2 type / TFIIH subunit Tfb4/GTF2H3 / Transcription factor TFIIH subunit p52/Tfb2 / TFIIH C1-like domain / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / von Willebrand factor, type A / RAD3/XPD family / Helicase, C-terminal ...TFIIH C1-like domain / Helicase conserved C-terminal domain / Helicase-like, DEXD box c2 type / TFIIH subunit Tfb4/GTF2H3 / Transcription factor TFIIH subunit p52/Tfb2 / TFIIH C1-like domain / DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site / von Willebrand factor, type A / RAD3/XPD family / Helicase, C-terminal / Helicase XPB/Ssl2 / ERCC3/RAD25/XPB C-terminal helicase / Helicase/UvrB, N-terminal / DEAH-box subfamily ATP-dependent helicases signature. / VWFA domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-2 domain profile. / Helicase C-terminal domain / Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Formation of HIV elongation complex in the absence of HIV Tat / Formation of the HIV-1 Early Elongation Complex / ATP-dependent helicase, C-terminal / Ssl1-like / HIV Transcription Initiation / Helicase XPB/Ssl2, N-terminal domain / Helical and beta-bridge domain / DEAD_2 / Transcription factor TFIIH complex subunit Tfb5 / Type III restriction enzyme, res subunit / Ssl1-like / Transcription factor Tfb4 / Transcription factor Tfb2 / von Willebrand factor A-like domain superfamily / TFB5-like superfamily / ERCC3/RAD25/XPB helicase, C-terminal domain / TFIIH subunit TTDA/Tfb5 / P-loop containing nucleoside triphosphate hydrolase / Helicase superfamily 1/2, ATP-binding domain, DinG/Rad3-type / Helicase superfamily 1/2, ATP-binding domain / Zinc finger C2H2-type / Zinc finger, RING/FYVE/PHD-type / ATP-dependent helicase Rad3/Chl1-like / TFIIH subunit Ssl1/p44 / Helical and beta-bridge domain / DEAD2 / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / Superfamilies 1 and 2 helicase C-terminal domain profile. / RNA Polymerase I Chain Elongation / Gap-filling DNA repair synthesis and ligation in TC-NER / RNA Polymerase II Transcription Initiation And Promoter Clearance / Formation of Incision Complex in GG-NER / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / Formation of TC-NER Pre-Incision Complex / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Dual incision in TC-NER / RNA Pol II CTD phosphorylation and interaction with CE / RNA Polymerase II Transcription Elongation / RNA Polymerase II Pre-transcription Events / Cytosolic iron-sulfur cluster assembly / NoRC negatively regulates rRNA expression / TP53 Regulates Transcription of DNA Repair Genes / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / mRNA Capping / Dual Incision in GG-NER / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / Transcription of the HIV genome / RNA Polymerase II HIV Promoter Escape / RNA Polymerase II Promoter Escape / RNA Polymerase I Transcription Termination / MMXD complex / core TFIIH complex portion of holo TFIIH complex / nucleotide-excision repair, DNA duplex unwinding / central nervous system myelin formation / 5'-3' DNA helicase activity / erythrocyte maturation / hair follicle maturation / 3'-5' DNA helicase activity / hair cell differentiation / core TFIIH complex / holo TFIIH complex / embryonic cleavage / regulation of mitotic cell cycle phase transition / hematopoietic stem cell differentiation / G-protein coupled receptor internalization / phosphorylation of RNA polymerase II C-terminal domain / translation factor activity, RNA binding / rDNA binding / transcription elongation from RNA polymerase I promoter / transcription initiation from RNA polymerase I promoter / UV protection / termination of RNA polymerase I transcription / transcription factor TFIID complex / embryonic organ development / ATP-dependent DNA helicase activity / nucleotide-excision repair, preincision complex stabilization / spinal cord development
Function and homology information
SourceHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / 4.4 Å resolution
AuthorsGreber BJ / Nguyen THD / Fang J / Afonine PV / Adams PD / Nogales E
CitationJournal: Nature / Year: 2017
Title: The cryo-electron microscopy structure of human transcription factor IIH.
Authors: Basil J Greber / Thi Hoang Duong Nguyen / Jie Fang / Pavel V Afonine / Paul D Adams / Eva Nogales
DateDeposition: Jul 10, 2017 / Header (metadata) release: Jul 26, 2017 / Map release: Oct 4, 2017 / Last update: Feb 14, 2018

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.027
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.027
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

Fileemd_8817.map.gz (map file in CCP4 format, 67109 KB)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
256 pix
1.32 Å/pix.
= 337.92 Å
256 pix
1.32 Å/pix.
= 337.92 Å
256 pix
1.32 Å/pix.
= 337.92 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.32 Å
Density
Contour Level:0.027 (by author), 0.027 (movie #1):
Minimum - Maximum-0.06940234 - 0.1495091
Average (Standard dev.)-8.039855E-6 (0.00466946)
Details

EMDB XML:

Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions256256256
Origin000
Limit255255255
Spacing256256256
CellA=B=C: 337.92 Å
α=β=γ: 90 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.321.321.32
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z337.920337.920337.920
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ281156
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.0690.150-0.000

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Supplemental data

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Sample components

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Entire Transcription factor IIH (TFIIH)

EntireName: Transcription factor IIH (TFIIH) / Number of components: 1
MassTheoretical: 490 kDa

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Component #1: protein, Transcription factor IIH (TFIIH)

ProteinName: Transcription factor IIH (TFIIH) / Recombinant expression: No
MassTheoretical: 490 kDa
SourceSpecies: Homo sapiens (human) / Strain: HeLa
Source (natural)Organelle: Nucleus / Location in cell: Nucleus

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Experimental details

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Sample preparation

SpecimenSpecimen state: particle / Method: cryo EM
Sample solutionSpecimen conc.: 0.0049 mg/ml / pH: 7.8
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 278.15 K / Humidity: 100 % / Details: 3-4 minute incubation, 2 second blot

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Electron microscopy imaging

ImagingMicroscope: FEI TITAN
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 40 e/Å2 / Illumination mode: FLOOD BEAM
LensMagnification: 37879 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 2000 - 4500 nm
Specimen HolderModel: GATAN LIQUID NITROGEN
CameraDetector: GATAN K2 (4k x 4k)

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Image acquisition

Image acquisitionNumber of digital images: 8300 / Sampling size: 5 microns
Details: 8300 micrographs collected in four session with identical acquisition settings. Sessions lasted 4, 2, 4, and 4 days and yielded 1200, 1700, 2800, and 2600 micrographs.

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Image processing

ProcessingMethod: single particle reconstruction / Number of projections: 88700
Details: Micrographs were inspected for quality of Thon rings and ice contamination. Poor micrographs were rejected.
3D reconstructionAlgorithm: FOURIER SPACE / Software: RELION
CTF correction: Correction within RELION based on values determined in CTFFIND4.
Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF
Details: RELION 3D auto-refinement (gold standard). The final 3D classification used signal-subtracted particle images. The final reconstruction used the corresponding un-subtracted particle images.
Euler angles: Maximum-likelihood 3D refinement within RELION.

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