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- EMDB-4336: Structure of two molecules of the chromatin remodelling enzyme Ch... -

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Basic information

Entry
Database: EMDB / ID: EMD-4336
TitleStructure of two molecules of the chromatin remodelling enzyme Chd1 bound to a nucleosome
Map data
Sample
  • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
    • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
      • Protein or peptide: Histone H3
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
    • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
      • DNA: DNA (176-MER)
      • DNA: DNA (177-MER)
    • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
      • Protein or peptide: Chromo domain-containing protein 1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: BERYLLIUM TRIFLUORIDE ION
Function / homology
Function and homology information


nucleolar chromatin / regulation of transcriptional start site selection at RNA polymerase II promoter / negative regulation of DNA-templated DNA replication / regulation of chromatin organization / rDNA binding / SLIK (SAGA-like) complex / DNA double-strand break processing / nucleosome organization / SAGA complex / sister chromatid cohesion ...nucleolar chromatin / regulation of transcriptional start site selection at RNA polymerase II promoter / negative regulation of DNA-templated DNA replication / regulation of chromatin organization / rDNA binding / SLIK (SAGA-like) complex / DNA double-strand break processing / nucleosome organization / SAGA complex / sister chromatid cohesion / ATP-dependent chromatin remodeler activity / termination of RNA polymerase II transcription / termination of RNA polymerase I transcription / ATP-dependent activity, acting on DNA / methylated histone binding / DNA-templated transcription initiation / helicase activity / transcription elongation by RNA polymerase II / double-strand break repair via homologous recombination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / chromatin DNA binding / structural constituent of chromatin / nucleosome / nucleosome assembly / site of double-strand break / histone binding / transcription cis-regulatory region binding / chromatin remodeling / protein heterodimerization activity / chromatin binding / chromatin / regulation of transcription by RNA polymerase II / ATP hydrolysis activity / mitochondrion / DNA binding / ATP binding / nucleus
Similarity search - Function
Chromodomain helicase DNA-binding domain / Chromodomain helicase DNA-binding domain 1 / Chromodomain-helicase-DNA-binding protein 1-like, C-terminal domain / Chromodomain-helicase-DNA-binding protein 1-like, C-terminal / DUF4208 / Chromo domain, conserved site / Chromo domain signature. / Chromo domain / Chromo (CHRromatin Organisation MOdifier) domain / Chromo and chromo shadow domain profile. ...Chromodomain helicase DNA-binding domain / Chromodomain helicase DNA-binding domain 1 / Chromodomain-helicase-DNA-binding protein 1-like, C-terminal domain / Chromodomain-helicase-DNA-binding protein 1-like, C-terminal / DUF4208 / Chromo domain, conserved site / Chromo domain signature. / Chromo domain / Chromo (CHRromatin Organisation MOdifier) domain / Chromo and chromo shadow domain profile. / Chromo/chromo shadow domain / Chromatin organization modifier domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Chromo-like domain superfamily / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / Histone H2A / Histone 2A / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H3 signature 1. / Helicase conserved C-terminal domain / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Homeobox-like domain superfamily / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Histone H4 / Histone H2A type 1 / Chromo domain-containing protein 1 / Histone H4 / Histone H3
Similarity search - Component
Biological speciesXenopus laevis (African clawed frog) / synthetic construct (others) / Saccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 10.0 Å
AuthorsSundaramoorthy R / Owen-hughes T / Norman DG / Hughes A
CitationJournal: Elife / Year: 2018
Title: Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome.
Authors: Ramasubramanian Sundaramoorthy / Amanda L Hughes / Hassane El-Mkami / David G Norman / Helder Ferreira / Tom Owen-Hughes /
Abstract: ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein-DNA interactions. Here, we present structures of the ...ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein-DNA interactions. Here, we present structures of the Chd1 protein engaged with nucleosomes in the presence of the transition state mimic ADP-beryllium fluoride. The path of DNA strands through the ATPase domains indicates the presence of contacts conserved with single strand translocases and additional contacts with both strands that are unique to Snf2 related proteins. The structure provides connectivity between rearrangement of ATPase lobes to a closed, nucleotide bound state and the sensing of linker DNA. Two turns of linker DNA are prised off the surface of the histone octamer as a result of Chd1 binding, and both the histone H3 tail and ubiquitin conjugated to lysine 120 are re-orientated towards the unravelled DNA. This indicates how changes to nucleosome structure can alter the way in which histone epitopes are presented.
History
DepositionMar 19, 2018-
Header (metadata) releaseAug 22, 2018-
Map releaseAug 22, 2018-
UpdateNov 21, 2018-
Current statusNov 21, 2018Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.044
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.044
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  • Surface view with fitted model
  • Atomic models: PDB-6g0l
  • Surface level: 0.044
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4336.png

Downloads & links

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Map

FileDownload / File: emd_4336.map.gz / Format: CCP4 / Size: 67 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.42 Å/pix.
x 260 pix.
= 369.2 Å		1.42 Å/pix.
x 260 pix.
= 369.2 Å		1.42 Å/pix.
x 260 pix.
= 369.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.42 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy SOFTWARE: 0.044 / Movie #1: 0.044
Minimum - Maximum-0.04725074 - 0.16230749
Average (Standard dev.)0.00074962294 (±0.00789947)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions260260260
Spacing260260260
CellA=B=C: 369.19998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.421.421.42
M x/y/z260260260
origin x/y/z0.0000.0000.000
length x/y/z369.200369.200369.200
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS260260260
D min/max/mean-0.0470.1620.001

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Supplemental data

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Sample components

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Entire : X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1

EntireName: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
Components
  • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
    • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
      • Protein or peptide: Histone H3
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
    • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
      • DNA: DNA (176-MER)
      • DNA: DNA (177-MER)
    • Complex: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
      • Protein or peptide: Chromo domain-containing protein 1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: BERYLLIUM TRIFLUORIDE ION

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Supramolecule #1: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1

SupramoleculeName: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Molecular weightTheoretical: 600 KDa

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Supramolecule #2: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1

SupramoleculeName: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#5
Source (natural)Organism: Xenopus laevis (African clawed frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Supramolecule #3: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1

SupramoleculeName: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
type: complex / ID: 3 / Parent: 1 / Macromolecule list: #6-#7
Source (natural)Organism: synthetic construct (others)

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Supramolecule #4: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1

SupramoleculeName: X. laevis nucleosome pn 601 DNA with S.cerevisiae remodeller Chd1
type: complex / ID: 4 / Parent: 1 / Macromolecule list: #8
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Macromolecule #1: Histone H3

MacromoleculeName: Histone H3 / type: protein_or_peptide / ID: 1
Details: Histone H3 sequence from X. Laevis. The N-terminal region from 1-39 is not resolved.
Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.407075 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVGLFEDTN LCGIHAKRVT IMPKDIQLAR RIRGERA

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Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 2
Details: Histone H4 sequence from X. Laevis. The N-terminal region from 1-19 is not resolved.
Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 11.394426 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

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Macromolecule #3: Histone H2A type 1

MacromoleculeName: Histone H2A type 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 14.193578 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVR NDEELNKLLG RVTIAQGRVL PNIQSVLLPK KTESAKSAKS K

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Macromolecule #4: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 13.939228 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPDPAKSAPA AKKGSKKAVT KTQKKDGKKR RKTRKESYAI YVYKVLKQVH PDTGISSKAM SIMNSFVNDV FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSAK

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Macromolecule #5: Histone H2A type 1

MacromoleculeName: Histone H2A type 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 14.093436 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVR NDEELNKLLG RVTIAQGGVL PNIQSVLLPK KTESAKSAKS K

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Macromolecule #8: Chromo domain-containing protein 1

MacromoleculeName: Chromo domain-containing protein 1 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Molecular weightTheoretical: 168.496609 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR KRMTTIEDDE DEFEDEEGEE DSGEDEDEED FEEDDDYYG SPIKQNRSKP KSRTKSKSKS KPKSQSEKQS TVKIPTRFSN RQNKTVNYNI DYSDDDLLES EDDYGSEEAL S EENVHEAS ...String:
MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR KRMTTIEDDE DEFEDEEGEE DSGEDEDEED FEEDDDYYG SPIKQNRSKP KSRTKSKSKS KPKSQSEKQS TVKIPTRFSN RQNKTVNYNI DYSDDDLLES EDDYGSEEAL S EENVHEAS ANPQPEDFHG IDIVINHRLK TSLEEGKVLE KTVPDLNNCK ENYEFLIKWT DESHLHNTWE TYESIGQVRG LK RLDNYCK QFIIEDQQVR LDPYVTAEDI EIMDMERERR LDEFEEFHVP ERIIDSQRAS LEDGTSQLQY LVKWRRLNYD EAT WENATD IVKLAPEQVK HFQNRENSKI LPQYSSNYTS QRPRFEKLSV QPPFIKGGEL RDFQLTGINW MAFLWSKGDN GILA DEMGL GKTVQTVAFI SWLIFARRQN GPHIIVVPLS TMPAWLDTFE KWAPDLNCIC YMGNQKSRDT IREYEFYTNP RAKGK KTMK FNVLLTTYEY ILKDRAELGS IKWQFMAVDE AHRLKNAESS LYESLNSFKV ANRMLITGTP LQNNIKELAA LVNFLM PGR FTIDQEIDFE NQDEEQEEYI HDLHRRIQPF ILRRLKKDVE KSLPSKTERI LRVELSDVQT EYYKNILTKN YSALTAG AK GGHFSLLNIM NELKKASNHP YLFDNAEERV LQKFGDGKMT RENVLRGLIM SSGKMVLLDQ LLTRLKKDGH RVLIFSQM V RMLDILGDYL SIKGINFQRL DGTVPSAQRR ISIDHFNSPD SNDFVFLLST RAGGLGINLM TADTVVIFDS DWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDL NLDDVLNHAE DHVTTPDLGE SHLGGEEFLK QFEVTDYKAD IDWDDIIPEE ELKKLQDEEQ KRKDEEYVKE Q LEMMNRRD NALKKIKNSV NGDGTAANSD SDDDSTSRSS RRRARANDMD SIGESEVRAL YKAILKFGNL KEILDELIAD GT LPVKSFE KYGETYDEMM EAAKDCVHEE EKNRKEILEK LEKHATAYRA KLKSGEIKAE NQPKDNPLTR LSLKKREKKA VLF NFKGVK SLNAESLLSR VEDLKYLKNL INSNYKDDPL KFSLGNNTPK PVQNWSSNWT KEEDEKLLIG VFKYGYGSWT QIRD DPFLG ITDKIFLNEV HNPVAKKSAS SSDTTPTPSK KGKGITGSSK KVPGAIHLGR RVDYLLSFLR GGLNTKSPSA DIGSK KLPT GPSKKRQRKP ANHSKSMTPE ITSSEPANGP PSKRMKALPK GPAALINNTR LSPNSPTPPL KSKVSRDNGT RQSSNP SSG SAHEKEYDSM DEEDCRHTMS AIRTSLKRLR RGGKSLDRKE WAKILKTELT TIGNHIESQK GSSRKASPEK YRKHLWS YS ANFWPADVKS TKLMAMYDKI TESQKK

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Macromolecule #6: DNA (176-MER)

MacromoleculeName: DNA (176-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 54.088469 KDa
SequenceString: (DA)(DT)(DA)(DC)(DG)(DC)(DG)(DG)(DC)(DC) (DG)(DC)(DC)(DC)(DA)(DT)(DC)(DA)(DG)(DA) (DA)(DT)(DC)(DC)(DC)(DG)(DG)(DT)(DG) (DC)(DC)(DG)(DA)(DG)(DG)(DC)(DC)(DG)(DC) (DT) (DC)(DA)(DA)(DT)(DT)(DG) ...String:
(DA)(DT)(DA)(DC)(DG)(DC)(DG)(DG)(DC)(DC) (DG)(DC)(DC)(DC)(DA)(DT)(DC)(DA)(DG)(DA) (DA)(DT)(DC)(DC)(DC)(DG)(DG)(DT)(DG) (DC)(DC)(DG)(DA)(DG)(DG)(DC)(DC)(DG)(DC) (DT) (DC)(DA)(DA)(DT)(DT)(DG)(DG)(DT) (DC)(DG)(DT)(DA)(DG)(DA)(DC)(DA)(DG)(DC) (DT)(DC) (DT)(DA)(DG)(DC)(DA)(DC)(DC) (DG)(DC)(DT)(DT)(DA)(DA)(DA)(DC)(DG)(DC) (DA)(DC)(DG) (DT)(DA)(DC)(DG)(DC)(DG) (DC)(DT)(DG)(DT)(DC)(DC)(DC)(DC)(DC)(DG) (DC)(DG)(DT)(DT) (DT)(DT)(DA)(DA)(DC) (DC)(DG)(DC)(DC)(DA)(DA)(DG)(DG)(DG)(DG) (DA)(DT)(DT)(DA)(DC) (DT)(DC)(DC)(DC) (DT)(DA)(DG)(DT)(DC)(DT)(DC)(DC)(DA)(DG) (DG)(DC)(DA)(DC)(DG)(DT) (DG)(DT)(DC) (DA)(DG)(DA)(DT)(DA)(DT)(DA)(DT)(DA)(DC) (DA)(DT)(DC)(DG)(DA)(DT)(DT) (DA)(DA) (DC)(DG)(DA)(DT)(DG)(DC)(DT)(DG)(DG)(DG) (DC)(DA)(DT)(DA)

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Macromolecule #7: DNA (177-MER)

MacromoleculeName: DNA (177-MER) / type: dna / ID: 7 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 54.885938 KDa
SequenceString: (DT)(DA)(DT)(DG)(DC)(DC)(DC)(DA)(DG)(DC) (DA)(DT)(DC)(DG)(DT)(DT)(DA)(DA)(DT)(DC) (DG)(DA)(DT)(DG)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DC)(DT)(DG)(DA)(DC)(DA)(DC)(DG) (DT) (DG)(DC)(DC)(DT)(DG)(DG) ...String:
(DT)(DA)(DT)(DG)(DC)(DC)(DC)(DA)(DG)(DC) (DA)(DT)(DC)(DG)(DT)(DT)(DA)(DA)(DT)(DC) (DG)(DA)(DT)(DG)(DT)(DA)(DT)(DA)(DT) (DA)(DT)(DC)(DT)(DG)(DA)(DC)(DA)(DC)(DG) (DT) (DG)(DC)(DC)(DT)(DG)(DG)(DA)(DG) (DA)(DC)(DT)(DA)(DG)(DG)(DG)(DA)(DG)(DT) (DA)(DA) (DT)(DC)(DC)(DC)(DC)(DT)(DT) (DG)(DG)(DC)(DG)(DG)(DT)(DT)(DA)(DA)(DA) (DA)(DC)(DG) (DC)(DG)(DG)(DG)(DG)(DG) (DA)(DC)(DA)(DG)(DC)(DG)(DC)(DG)(DT)(DA) (DC)(DG)(DT)(DG) (DC)(DG)(DT)(DT)(DT) (DA)(DA)(DG)(DC)(DG)(DG)(DT)(DG)(DC)(DT) (DA)(DG)(DA)(DG)(DC) (DT)(DG)(DT)(DC) (DT)(DA)(DC)(DG)(DA)(DC)(DC)(DA)(DA)(DT) (DT)(DG)(DA)(DG)(DC)(DG) (DG)(DC)(DC) (DT)(DT)(DC)(DG)(DG)(DC)(DA)(DC)(DC)(DG) (DG)(DG)(DA)(DT)(DT)(DC)(DT) (DG)(DA) (DT)(DG)(DG)(DG)(DC)(DG)(DG)(DC)(DC)(DG) (DC)(DG)(DT)(DA)(DT)

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Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #10: BERYLLIUM TRIFLUORIDE ION

MacromoleculeName: BERYLLIUM TRIFLUORIDE ION / type: ligand / ID: 10 / Number of copies: 2 / Formula: BEF
Molecular weightTheoretical: 66.007 Da
Chemical component information

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 7.5 / Component:
ConcentrationName
20.0 mMHepes
100.0 mMNaCl
GridModel: C-flat-1.2/1.3 4C / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK III
DetailsSample was gel filtration purified and it is monodisperse

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Electron microscopy

MicroscopeFEI TITAN KRIOS
TemperatureMin: 170.0 K / Max: 170.0 K
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 3870 pixel / Digitization - Dimensions - Height: 3870 pixel / Digitization - Sampling interval: 14.0 µm / Digitization - Frames/image: 5-28 / Number grids imaged: 1 / Number real images: 1800 / Average exposure time: 2.0 sec. / Average electron dose: 1.56 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated defocus max: 4.0 µm / Calibrated defocus min: 1.5 µm / Calibrated magnification: 98591 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 98591
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 250000
CTF correctionSoftware - Name: Gctf
Startup modelType of model: EMDB MAP
EMDB ID:

3502

Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 10.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 68000
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION
Final 3D classificationSoftware - Name: RELION
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: RECIPROCAL / Protocol: RIGID BODY FIT / Overall B value: 800 / Target criteria: Cross-correlation coefficient
Output model

PDB-6g0l:
Structure of two molecules of the chromatin remodelling enzyme Chd1 bound to a nucleosome

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  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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