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- EMDB-4271: Chloroplast F1Fo conformation 2 -

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Basic information

Entry
Database: EMDB / ID: EMD-4271
TitleChloroplast F1Fo conformation 2
Map datachloroplast ATP synthase conformation 2
Sample
  • Complex: Chloroplast ATP synthase
    • Protein or peptide: x 9 types
  • Ligand: x 3 types
Function / homology
Function and homology information


mitochondrial proton-transporting ATP synthase complex / chloroplast thylakoid membrane / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism ...mitochondrial proton-transporting ATP synthase complex / chloroplast thylakoid membrane / proton motive force-driven mitochondrial ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton transmembrane transporter activity / proton-transporting ATP synthase complex, catalytic core F(1) / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ADP binding / lipid binding / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
ATP synthase, F0 complex, subunit b' / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0) / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATPase, OSCP/delta subunit, conserved site / ATP synthase delta (OSCP) subunit signature. / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily ...ATP synthase, F0 complex, subunit b' / ATP synthase delta/epsilon subunit, C-terminal domain / ATP synthase, Delta/Epsilon chain, long alpha-helix domain / ATP synthase, F0 complex, subunit A, bacterial/chloroplast / ATP synthase, F0 complex, subunit b/b', bacterial/chloroplast / ATP synthase B/B' CF(0) / ATP synthase, F0 complex, subunit C, bacterial/chloroplast / ATPase, OSCP/delta subunit, conserved site / ATP synthase delta (OSCP) subunit signature. / F1F0 ATP synthase OSCP/delta subunit, N-terminal domain superfamily / ATP synthase, F0 complex, subunit A / ATP synthase, F0 complex, subunit A, active site / ATP synthase, F0 complex, subunit A superfamily / ATP synthase A chain / ATP synthase a subunit signature. / ATPase, OSCP/delta subunit / ATP synthase delta (OSCP) subunit / ATP synthase, F1 complex, delta/epsilon subunit / ATP synthase, F1 complex, delta/epsilon subunit, N-terminal / F0F1 ATP synthase delta/epsilon subunit, N-terminal / ATP synthase, Delta/Epsilon chain, beta-sandwich domain / ATP synthase, F0 complex, subunit C / F1F0 ATP synthase subunit C superfamily / ATP synthase, F0 complex, subunit C, DCCD-binding site / ATP synthase c subunit signature. / ATP synthase, F1 complex, gamma subunit conserved site / ATP synthase gamma subunit signature. / ATP synthase, F1 complex, beta subunit / ATP synthase, alpha subunit, C-terminal domain superfamily / ATP synthase, F1 complex, gamma subunit / ATP synthase, F1 complex, gamma subunit superfamily / ATP synthase / ATP synthase, alpha subunit, C-terminal / ATP synthase, F1 complex, alpha subunit / ATP synthase, F1 complex, alpha subunit nucleotide-binding domain / ATP synthase alpha/beta chain, C terminal domain / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP synthase subunit beta, chloroplastic / ATP synthase epsilon chain, chloroplastic / ATP synthase gamma chain, chloroplastic / ATP synthase subunit alpha, chloroplastic / ATP synthase subunit a, chloroplastic / ATP synthase subunit b, chloroplastic / ATP synthase delta chain, chloroplastic / ATP synthase subunit b', chloroplastic / ATP synthase subunit c, chloroplastic
Similarity search - Component
Biological speciesSpinacia oleracea (spinach) / Spinach (spinach)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsHahn A / Vonck J / Mills DJ / Meier T / Kuehlbrandt W
CitationJournal: Science / Year: 2018
Title: Structure, mechanism, and regulation of the chloroplast ATP synthase.
Authors: Alexander Hahn / Janet Vonck / Deryck J Mills / Thomas Meier / Werner Kühlbrandt /
Abstract: The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through ...The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded F motor drive ATP synthesis in the F head by rotary catalysis. We determined the high-resolution structure of the complete cFF complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a β-hairpin redox switch in subunit γ that blocks rotation in the dark.
History
DepositionJan 24, 2018-
Header (metadata) releaseFeb 28, 2018-
Map releaseMay 23, 2018-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.05
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  • Surface view colored by cylindrical radius
  • Surface level: 0.05
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  • Surface view with fitted model
  • Atomic models: PDB-6fkh
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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Structure viewerEM map:
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Supplemental images

emd_4271.png

Downloads & links

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Map

FileDownload / File: emd_4271.map.gz / Format: CCP4 / Size: 163.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationchloroplast ATP synthase conformation 2
Voxel sizeX=Y=Z: 1.053 Å
Density
Contour LevelBy AUTHOR: 0.05 / Movie #1: 0.05
Minimum - Maximum-0.1814016 - 0.26970923
Average (Standard dev.)0.0000915018 (±0.013628136)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions350350350
Spacing350350350
CellA=B=C: 368.55 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0531.0531.053
M x/y/z350350350
origin x/y/z0.0000.0000.000
length x/y/z368.550368.550368.550
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS350350350
D min/max/mean-0.1810.2700.000

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Supplemental data

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Mask #1

Fileemd_4271_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_4271_half_map_1.map
Projections & Slices
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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_4271_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Chloroplast ATP synthase

EntireName: Chloroplast ATP synthase
Components
  • Complex: Chloroplast ATP synthase
    • Protein or peptide: ATP synthase subunit a, chloroplastic
    • Protein or peptide: ATP synthase subunit alpha, chloroplastic
    • Protein or peptide: ATP synthase subunit beta, chloroplastic
    • Protein or peptide: ATP synthase epsilon chain, chloroplastic
    • Protein or peptide: ATP synthase gamma chain, chloroplastic
    • Protein or peptide: ATP synthase subunit c, chloroplastic
    • Protein or peptide: ATP synthase subunit b', chloroplastic
    • Protein or peptide: ATP synthase subunit b, chloroplastic
    • Protein or peptide: ATP synthase delta chain, chloroplastic
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Chloroplast ATP synthase

SupramoleculeName: Chloroplast ATP synthase / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Spinacia oleracea (spinach)
Molecular weightTheoretical: 600 KDa

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Macromolecule #1: ATP synthase subunit a, chloroplastic

MacromoleculeName: ATP synthase subunit a, chloroplastic / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 27.10268 KDa
SequenceString: MNVLSYSINP LKGLYAISGV EVGQHFYWQI GGFQIHGQVL ITSWVVIAIL LGSAAIAVRS PQTIPTGGQN FFEYVLEFIR DVSKTQIGE EYRPWVPFIG TMFLFIFVSN WSGALLPWKI IQLPHGELAA PTNDINTTVA LALLTSVAYF YAGLTKKGLG Y FGKYIQPT ...String:
MNVLSYSINP LKGLYAISGV EVGQHFYWQI GGFQIHGQVL ITSWVVIAIL LGSAAIAVRS PQTIPTGGQN FFEYVLEFIR DVSKTQIGE EYRPWVPFIG TMFLFIFVSN WSGALLPWKI IQLPHGELAA PTNDINTTVA LALLTSVAYF YAGLTKKGLG Y FGKYIQPT PILLPINILE DFTKPLSLSF RLFGNILADE LVVVVLVSLV PLVVPIPVMF LGLFTSGIQA LIFATLAAAY IG ESLEGHH

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Macromolecule #2: ATP synthase subunit alpha, chloroplastic

MacromoleculeName: ATP synthase subunit alpha, chloroplastic / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: H+-transporting two-sector ATPase
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 55.505199 KDa
SequenceString: MATIRADEIS KIIRERIEGY NREVKVVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT IGIALNLESN NVGVVLMGDG LMIQEGSSV KATGRIAQIP VSEAYLGRVI NALAKPIDGR GEITASESRL IESPAPGIMS RRSVYEPLQT GLIAIDAMIP V GRGQRELI ...String:
MATIRADEIS KIIRERIEGY NREVKVVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT IGIALNLESN NVGVVLMGDG LMIQEGSSV KATGRIAQIP VSEAYLGRVI NALAKPIDGR GEITASESRL IESPAPGIMS RRSVYEPLQT GLIAIDAMIP V GRGQRELI IGDRQTGKTA VATDTILNQQ GQNVICVYVA IGQKASSVAQ VVTNFQERGA MEYTIVVAET ADSPATLQYL AP YTGAALA EYFMYRERHT LIIYDDLSKQ AQAYRQMSLL LRRPPGREAY PGDVFYLHSR LLERAAKLSS LLGEGSMTAL PIV ETQAGD VSAYIPTNVI SITDGQIFLS ADLFNAGIRP AINVGISVSR VGSAAQIKAM KKVAGKLKLE LAQFAELEAF AQFA SDLDK ATQNQLARGQ RLRELLKQPQ SAPLTVEEQV MTIYTGTNGY LDSLELDQVR KYLVELRTYV KTNKPEFQEI ISSTK TFTE EAEALLKEAI QEQMERFLLQ EQA

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Macromolecule #3: ATP synthase subunit beta, chloroplastic

MacromoleculeName: ATP synthase subunit beta, chloroplastic / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO / EC number: H+-transporting two-sector ATPase
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 53.797367 KDa
SequenceString: MRINPTTSDP GVSTLEKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALIVK GRDTAGQPMN VTCEVQQLLG NNRVRAVAMS ATDGLTRGM EVIDTGAPLS VPVGGATLGR IFNVLGEPVD NLGPVDTRTT SPIHRSAPAF TQLDTKLSIF ETGIKVVDLL A PYRRGGKI ...String:
MRINPTTSDP GVSTLEKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALIVK GRDTAGQPMN VTCEVQQLLG NNRVRAVAMS ATDGLTRGM EVIDTGAPLS VPVGGATLGR IFNVLGEPVD NLGPVDTRTT SPIHRSAPAF TQLDTKLSIF ETGIKVVDLL A PYRRGGKI GLFGGAGVGK TVLIMELINN IAKAHGGVSV FGGVGERTRE GNDLYMEMKE SGVINEQNIA ESKVALVYGQ MN EPPGARM RVGLTALTMA EYFRDVNEQD VLLFIDNIFR FVQAGSEVSA LLGRMPSAVG YQPTLSTEMG SLQERITSTK EGS ITSIQA VYVPADDLTD PAPATTFAHL DATTVLSRGL AAKGIYPAVD PLDSTSTMLQ PRIVGEEHYE IAQRVKETLQ RYKE LQDII AILGLDELSE EDRLTVARAR KIERFLSQPF FVAEVFTGSP GKYVGLAETI RGFQLILSGE LDSLPEQAFY LVGNI DEAT AKAMNLEMES KLKK

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Macromolecule #4: ATP synthase epsilon chain, chloroplastic

MacromoleculeName: ATP synthase epsilon chain, chloroplastic / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 14.715707 KDa
SequenceString:
MTLNLCVLTP NRSIWNSEVK EIILSTNSGQ IGVLPNHAPT ATAVDIGILR IRLNDQWLTL ALMGGFARIG NNEITILVND AERGSDIDP QEAQQTLEIA EANLRKAEGK RQKIEANLAL RRARTRVEAS NTISS

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Macromolecule #5: ATP synthase gamma chain, chloroplastic

MacromoleculeName: ATP synthase gamma chain, chloroplastic / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 40.119066 KDa
SequenceString: MACSLSFSSS VSTFHLPTTT QSTQAPPNNA TTLPTTNPIQ CANLRELRDR IGSVKNTQKI TEAMKLVAAA KVRRAQEAVV NGRPFSETL VEVLYNMNEQ LQTEDVDVPL TKIRTVKKVA LMVVTGDRGL CGGFNNMLLK KAESRIAELK KLGVDYTIIS I GKKGNTYF ...String:
MACSLSFSSS VSTFHLPTTT QSTQAPPNNA TTLPTTNPIQ CANLRELRDR IGSVKNTQKI TEAMKLVAAA KVRRAQEAVV NGRPFSETL VEVLYNMNEQ LQTEDVDVPL TKIRTVKKVA LMVVTGDRGL CGGFNNMLLK KAESRIAELK KLGVDYTIIS I GKKGNTYF IRRPEIPVDR YFDGTNLPTA KEAQAIADDV FSLFVSEEVD KVEMLYTKFV SLVKSDPVIH TLLPLSPKGE IC DINGKCV DAAEDELFRL TTKEGKLTVE RDMIKTETPA FSPILEFEQD PAQILDALLP LYLNSQILRA LQESLASELA ARM TAMSNA TDNANELKKT LSINYNRARQ AKITGEILEI VAGANACV

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Macromolecule #6: ATP synthase subunit c, chloroplastic

MacromoleculeName: ATP synthase subunit c, chloroplastic / type: protein_or_peptide / ID: 6 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 7.977366 KDa
SequenceString:
MNPLIAAASV IAAGLAVGLA SIGPGVGQGT AAGQAVEGIA RQPEAEGKIR GTLLLSLAFM EALTIYGLVV ALALLFANPF V

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Macromolecule #7: ATP synthase subunit b', chloroplastic

MacromoleculeName: ATP synthase subunit b', chloroplastic / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 24.487596 KDa
SequenceString: MANMLVASSS KTLPTTTTTT ITPKPKFPLL KTPLLKLSPP QLPPLKHLNL SVLKSAAITA TPLTLSFLLP YPSLAEEIEK ASLFDFNLT LPIIMAEFLF LMFALDKIYY TPLGDFMDKR DASIKEQLSG VKDTSSEVKQ LEEQANAVMR AARAEISAAL N KMKKETQL ...String:
MANMLVASSS KTLPTTTTTT ITPKPKFPLL KTPLLKLSPP QLPPLKHLNL SVLKSAAITA TPLTLSFLLP YPSLAEEIEK ASLFDFNLT LPIIMAEFLF LMFALDKIYY TPLGDFMDKR DASIKEQLSG VKDTSSEVKQ LEEQANAVMR AARAEISAAL N KMKKETQL EVEAKLAEGR KKIEVELQEA LGSLEQQKED TIKSLDSQIS ALSDDIVKKV LPVS

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Macromolecule #8: ATP synthase subunit b, chloroplastic

MacromoleculeName: ATP synthase subunit b, chloroplastic / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 21.013904 KDa
SequenceString:
MKNVTDSFVF LGHWPSAGSF GFNTDILATN LINLSVVLGV LIFFGKGVLS DLLDNRKQRI LNTIRNSEEL RGKAIEQLEK ARARLKKVE MDADQFRVNG YSEIEREKMN LINSTYKTLE QFENYKNETI QFEQQKAINQ VRQRVFQQAL QGALGTLNSC L NNELHLRT INANIGMFGA MNEITD

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Macromolecule #9: ATP synthase delta chain, chloroplastic

MacromoleculeName: ATP synthase delta chain, chloroplastic / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Spinach (spinach)
Molecular weightTheoretical: 27.708582 KDa
SequenceString: MAALQNPVAL QSRTTTAVAA LSTSSTTSTP KPFSLSFSSS TATFNPLRLK ILTASKLTAK PRGGALGTRM VDSTASRYAS ALADVADVT GTLEATNSDV EKLIRIFSEE PVYYFFANPV ISIDNKRSVL DEIITTSGLQ PHTANFINIL IDSERINLVK E ILNEFEDV ...String:
MAALQNPVAL QSRTTTAVAA LSTSSTTSTP KPFSLSFSSS TATFNPLRLK ILTASKLTAK PRGGALGTRM VDSTASRYAS ALADVADVT GTLEATNSDV EKLIRIFSEE PVYYFFANPV ISIDNKRSVL DEIITTSGLQ PHTANFINIL IDSERINLVK E ILNEFEDV FNKITGTEVA VVTSVVKLEN DHLAQIAKGV QKITGAKNVR IKTVIDPSLV AGFTIRYGNE GSKLVDMSVK KQ LEEIAAQ LEMDDVTLAV

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Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 5 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #11: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 11 / Number of copies: 3 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

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Macromolecule #12: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 12 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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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

BufferpH: 8
Component:
ConcentrationNameFormula
30.0 mMHEPES
2.0 mMMgCl2
0.5 mMEDTAEthylenediaminetetraacetic acid
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 70 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsCalibrated defocus max: 2.5 µm / Calibrated defocus min: 1.5 µm / Calibrated magnification: 132953 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 75000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number real images: 6254 / Average exposure time: 62.0 sec. / Average electron dose: 25.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 670614
CTF correctionSoftware - Name: CTFFIND (ver. 4)
Startup modelType of model: OTHER
Details: unpublished ab initio reconstruction from data from another microscope
Initial angle assignmentType: OTHER / Software - Name: RELION (ver. 2.1)
Final 3D classificationNumber classes: 3 / Avg.num./class: 70000 / Software - Name: RELION (ver. 2.1)
Details: three classes with 167,000, 15,000 and 14,000 particles. This is the second one.
Final angle assignmentType: OTHER / Software - Name: RELION (ver. 2.1)
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.1) / Number images used: 15395
FSC plot (resolution estimation)

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Atomic model buiding 1

Detailsrigid body fit from structure build in complex in conformation 1
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-6fkh:
Chloroplast F1Fo conformation 2

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